Chymotrypsin

Critical Reviews in Biochemistry and Molecular Biology

Volumn 1, Issue 2, 1973, Pages 149-199

  Bender, M L ^a   Killheffer, J V ^b   Cohen, S ^c  

^a NORTHWESTERN UNIVERSITY   (United States)

^b Encyclopedia Britannica   (United States)

^c BRANDEIS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BENZENESULFONIC ACID DERIVATIVE; CHYMOTRYPSIN; CHYMOTRYPSINOGEN; MESYLIC ACID DERIVATIVE; NITROPHENOL;

ANIMAL; BINDING SITE; CATTLE; CHEMICAL STRUCTURE; CHICKEN; COMPARATIVE STUDY; DOGFISH; ENZYME ACTIVATION; ENZYMOLOGY; FISH; FROGS AND TOADS; HUMAN; KINETICS; METABOLISM; PANCREAS; PH; PROTEIN BINDING; PROTEIN CONFORMATION; RAT; REVIEW; SPECIES DIFFERENCE; SWINE; TURTLE;

AMINO ACIDS; ANIMAL; ANURA; BENZENESULFONATES; BINDING SITES; CATTLE; CHICKENS; CHYMOTRYPSIN; CHYMOTRYPSINOGEN; COMPARATIVE STUDY; DOGFISH; ENZYME ACTIVATION; FISHES; HUMAN; HYDROGEN-ION CONCENTRATION; KINETICS; MESYLATES; MODELS, MOLECULAR; NITROPHENOLS; PANCREAS; PROTEIN BINDING; PROTEIN CONFORMATION; RATS; SPECIES SPECIFICITY; SWINE; TURTLES;

EID: 0015613107     PISSN: 10409238     EISSN: None     Source Type: Journal    
DOI: 10.3109/10409237309102546     Document Type: Article

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74. On the interaction of the active site of α-chymotrypsin, with chromophores: proflavin binding and enzyme conformation during catalysi
75. Spectral studies of the interaction of α-chymotrypsin, and trypsin with proflavin
76. The optical detection of transients in trypsin- and chymotrypsin-catalyzed reaction
77. Comparative binding properties of native and anhydro chymotrypsins determined by a competitive dialysis metho
78. The specific binding of Biebrich scarlet to the active site of α-chymotrypsi
79. Enzyme actio
80. General theory of the action of some diastase
81. Kinetics of invertase actio
82. A note on the kinetics of enzyme actio
83. Hematin compound of peroxidas
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85. The kinetics of the enzyme-substrate compound of peroxidas
86. The properties of the enzyme-substrate compounds of horseradish and lacto-peroxidas
87. The interaction of myosin with adenosine triphosphat
88. The number of catalytically active sites present on the chymotrypsin molecul
89. The binding of inhibitors to α-chymotrypsi
90. Structure of crystalline α-chymotrypsin. III. Crystallographic studies of substrates and inhibitors bound to the active site of α-chymotrypsi
91. Interaction of aromatic compounds with α-chymotrypsi
92. Equilibrium and rate constants for the interconversion of two conformations of α-chymotrypsin. The existence of a catalytically inactive conformation at neutral p
93. Binding properties of oligomeric α-chymotrypsi
94. Interaction of δ-chymotrypsin with proflavin
95. Specific binding of thionine to the active site of trypsi
96. Amino acids involved in the action of chymotrypsi
97. Molecular conformation of chymotrypsinogen and chymotrypsin by low-angle x-ray diffractio
98. Measurement of protein-binding phenomena by gel filtratio
99. The active centre of chymotrypsi
100. Sulfonyl fluorides as inhibitors of esterases. III. Identification of serine as the site of sulfonylation in phenylmethanesulfonyl-α-chymotrypsi
101. The combination of chymotrypsin and chymotrypsinogen with fluorescent substrates and inhibitors for chymotrypsi
102. Reaction mechanism of some proteolytic enzyme
103. Acetylcholinesterase. X. Mechanism of the catalysis of acylation reaction
104. The cholinesterase-inhibiting action of fluorophosphonate
105. The inhibition of serum cholinesterase by alkyl fluorophosphate
106. The specific esterase activity of trypsi
107. The specific esterase activities of chymotrypsi
108. Inhibition of the proteinase and esterase activities of trypsin and chymotrypsin by diisopropyl fluorophosphate: crystallization of inhibited chymotrypsi
109. The inhibition of chymotrypsin by diethyl p-nitrophenyl phosphat
110. The reaction of p-nitrophenyl esters with chymotrypsin and insuli
111. New developments in the chemistry of war gase
112. Toxic phosphorus and fluorine compound
113. The reaction of organophosphorus compounds with hydrolytic enzymes. III. The inhibition of chymotrypsin and trypsi
114. Mode of inhibition of chymotrypsin by diisopropyl fluorophosphate. I. Introduction of phosphoru
115. Reactivation of diethyl p-nitrophenyl phosphate-inhibited α-chymotrypsin by hydroxylamin
116. Reactivation of α-chymotrypsin inhibited by organic phosphate
117. Molecular complementariness as basis for reactivation of alkyl phosphate-inhibited enzyme
118. The reactivation of phosphorylated chymotrypsi
119. Studies on the reactivation of diethylphosphorylchymotrypsi
120. Inhibition of esterases by the fluorides of organic acid
121. Sulfonyl fluorides as inhibitors of esterases. I. Rates of reaction with acetylcholinesterase, chymotrypsin, and trypsi
122. The study of α-chymotrypsin by x-ray diffractio
123. An x-ray diffraction study of inhibited derivatives of α-chymotrypsi
124. Enzymatic and nonenzymatic reactions of cyclic sulfonate and sulfate ester
125. The mechanism of the reaction of chymotrypsin with p-nitrophenyl acetat
126. The mechanism of chymotrypsin-catalyzed, reactions. II
127. Acetyl chymotrypsi
128. Acetyl chymotrypsin and its reaction with ethano
129. The reaction of p-nitrophenol acetate with chymotrypsi
130. An intermediate in the deacetylation of monoacetyl-δ-chymotrypsin having the properties of acetyl-imidazoly
131. Acylation of the enzymatic site of δ-chymotrypsin by esters, acid anhydrides, and acid chloride
132. Enzyme model
133. The nature of the reaction between diisopropylfluorophosphate and chymotrypsi
134. Isolation of acetyl peptides from acetyl chymotrypsi
135. Crystallization and some properties of trimethylacetyl chymotrypsi
136. Spectrophotometric investigations of the mechanism of α-chymotrypsin-catalyzed hydrolyses. Detection of the acyl-enzyme intermediat
137. The formation of an acyl-enzyme intermediate in the α-chymotrypsin-catalyzed hydrolyses of non-labile trans-cinnamic acid ester
138. Influence of pH on rates of enzymatic reactions. IV. Hydrolysis of methyl hydrocinnamate catalyzed by α-chymotrypsi
139. The spectrophotometric determination of the operational normality of an α-chymotrypsin solutio
140. The determination of the concentration of hydrolytic enzyme solutions: α-chymotrypsin, trypsin, papain, elastase, subtilisin, and acetylcholinesteras
141. Principles of active site titration of proteolytic enzymes, Chap
142. The pH-dependence of some α-chymotrypsin-catalyzed hydrolyse
143. The mechanism of α-chymotrypsin-catalyzed hydrolyse
144. The current status of the α-chymotrypsin mechanis
145. Kinetics of the system α-chymotrypsin: methyl hippurate: water: hydroxylamine; the role of water in enzymatic hydrolysi
146. Evidence for the formation of hippuryl chymotrypsin during the hydrolysis of hippuric acid ester
147. Oxazolinones as enzyme acylating agent
148. The apparent absence of an acyl-enzyme intermediate in the chymotrypsin-catalyzed hydrolysis of acetyl-L-tyrosine hydroxamic aci
149. The apparent absence of an acyl-enzyme intermediate in certain chymotrypsin-catalyzed reactions - a correctio
150. The chymotrypsin-catalyzed hydrolysis and synthesis of N-acetyl-L-tyrosine hydroxamic aci
151. On the question of an acyl-enzyme intermediate in the chymotrypsin-catalyzed hydrolysis of hydroxamic acid
152. The α-chymotrypsin-catalyzed hydrolysis and hydroxylaminolysis of N-acetyl-L-tyrosine ethyl este
153. The α-chymotrypsin-catalyzed hydrolysis and hydroxylaminolysis of acetyltyrosine p-nitroanilid
154. Evidence against the obligatory formation of an acyl enzyme intermediate in the α-chymotrypsin-catalyzed reactions of amide
155. The kinetic consequences of the acyl enzyme mechanism for the reactions of specific substrate
156. The observation of acyl-enzyme intermediates in the α-chymotrypsin-catalyzed reactions of N-acetyl-L-tryptophan derivatives at low p
157. Optical and chemical identification of kinetic steps in trypsin- and chymotrypsin-catalyzed reaction
158. Determination of the binding constant of a specific ester and a specific amide substrate to α-chymotrypsi
159. Investigations of the chymotrypsin-catalyzed hydrolysis of specific substrates. III. Determination of individual rate constants and enzyme-substrate binding constants for specific amide and ester substrate
160. The direct observation of an acyl-enzyme intermediate in the α-chymotrypsin-catalyzed hydrolysis of a specific substrate at neutral p
161. Carbonyl oxygen exchange in general base-catalyzed ester hydrolysi
162. Proposed mechanism of action of hydrolytic enzyme
163. Acylation of the enzymatic site of 6-chymotrypsin by ester, acid anhydrides, and acid chloride
164. The effect of substituents on the deacylation of benzoyl-chymotrypsin
165. The concurrent alkaline hydrolysis and isotopic oxygen exchange of a series of para-substituted methyl benzoate
166. α-Chymotrypsin-catalyzed hydrolysis of N-furylacryloyl-tyrosine derivative
167. Intramolecular S-O and S-N acetyl transfer reaction
168. Oxygen exchange as evidence for the existence of an intermediate in ester hydrolysi
169. The kinetics of alkaline hydrolysis and n-buylaminolysis of ethyl-p-nitrobenzoate and ethyl-p-nitrothiolbenzoat
170. Carbonyl oxygen exchange in general base-catalyzed ester hydrolysi
171. Kinetics of hydrolysis of p-nitrophenyl thiolacetate by chymotrypsi
172. Substituent effects of the chymotrypsin-catalyzed hydrolysis of specific ester substrate
173. The effect of structure on the rates of some α-chymotrypsin-catalyzed reaction
174. The kinetics of the α-chymotrypsin-catalyzed hydrolysis of p-nitrophenyl acetat
175. An electrophilic mechanism in the chymotrypsin-catalyzed hydrolysis of anilide substrate
176. On the mechanism of action at the acylation step of the chymotrypsin-catalyzed hydrolysis of anilide
177. The concurrent alkaline hydrolysis and isotopic oxygen exchange of a series of para-substituted acetanilide
178. Chymotrypsin-catalyzed hydrolysis of m-, p-, and o-nitroanilides of N-benzoyl-L-tyrosin
179. Participation of an acidic group in the chymotrypsin-catalysi
180. m. Detection of an intermediat
181. The correlation of the pH (pD) dependence and the stepwise mechanism of α-chymotrypsin-catalyzed reaction
182. The imidazole-catalyzed hydrolysis of p-nitrophenyl acetat
183. Imidazole catalysis. II. The reaction of substituted imidazoles with phenyl acetates in aqueous solutio
184. Reactivity and catalysis in reactions of the serine hydroxyl group and of O-acyl serine
185. General base catalysis of ester hydrolysi
186. An intermediate in the deacetylation of mono-acetyl-δ-chymotrypsin having the properties of acetyl-imidazol
187. Acylation of chymotrypsin by active esters of nonspecific substrates. Evidence for a transient acylimidazole intermediat
188. Oxazolinones as enzyme acylating agent
189. On the spontaneous and enzyme-catalyzed hydrolysis of saturated oxazolinone
190. On the spontaneous and α-chymotrypsin-catalyzed hydrolysis of 4-cis-benzylidene-2-phenyloxazolin-5-one. Catalysis by tris (hydroxymethyl) aminomethan
191. Intramolecular reaction of specific substrate as a step in α-chymotrypsin catalyzed hydrolysi
192. α-Chymotrypsin-catalyzed hydrolysis of N-furylacryloyl-tyrosine derivative
193. Optical and chemical identification of kinetic steps in trypsin and chymotrypsin-catalyzed reaction
194. Intramolecular dehydration of phenylthiocarbamyl amino acids induced by α-chymotrypsi
195. The α-chymotrypsin-catalyzed hydrolysis of esters of a-amino acid
196. The active site in α-chymotrypsin. Absolute configuration and kinetics of hydrolysis of methyl-3, 4-dihydroisocoumarin-3-carboxylat
197. A possible mechanism of action of esterases inhibitable by organo-phosphorus compound
198. Co-operative effects of functional groups in peptides. I. Aspartyl-serine derivative
199. A possible role for arginine in enzyme mechanism
200. Studies on the active site of chymotrypsi
201. Structure of crystalline α-chymotrypsin. II. A preliminary report including a hypothesis for the activation mechanis
202. Structure of crystalline α-chymotrypsin. IV. The structure of indoleacryloyl-α-chymotrypsin and its relevance to the hydrolytic mechanism of the enzym
203. The correlation of the pH (pD) dependence and the stepwise mechanism of α-chymotrypsin-catalyzed reaction
204. The direct observation of an acyl-enzyme intermediate in the α-chymotrypsin-catalyzed hydrolysis of a specific substrate at neutral p
205. Alkaline pH dependence of δ-chymotrypsin-catalyzed hydrolysis of specific substrate
206. The difference between α- and δ-chymotrypsins. Preparation and alkaline pH dependence of α-chymotrypsin-catalyzed hydrolysis of N-acetyl-L-tryptophan methyl ester (ATME). The Involvement of alanine-149 in α-chymotrypsin catalysi
207. Structural changes in the activation of chymotrypsinoge
208. Substrate control of conformation characteristics in chymotrypsi
209. The alkaline pH dependence of chymotrypsin reactions. Postulation of a pH-dependent intramolecular competitive inhibitio
210. Investigations of the chymotrypsin-catalyzed hydrolysis of specific substrate
211. Conformational changes accompanying the formation of chymotrypsin-substrate complexes. Evidence for the involvement of an N-terminal α-amino group in the activity and the conformation of the enzym
212. Implication of an ionizing group in the control of conformation and activity of chymotrypsi
213. Spectrophotometric and kinetic evidence for the existence of at least two salt-dependent conformations of α-chymotrypsin at pH values near neutralit
214. Rate of ligand-promoted isomerization of proteins. Relaxation study of the “alkaline-transition” of δ-chymotrypsi
215. pH-Dependent proton absorption in chymotrypsin binding. Evidence for a pH-dependent conformation change of the enzym
216. Conformation and activity of chymotrypsin. The pH-dependent, substrate-induced proton uptak
217. pH-Dependent proton absorption in chymotrypsin. Small molecule interaction
218. Studies of the activity of chymotrypsi
219. Binding of competitive inhibitors to 6-chymotrypsin in the alkaline pH region. Competitive inhibition kinetics and proton-uptake measurement
220. Acylation of α- and δ-chymotrypsins by p-nitrophenyl acetat
221. The function of neighboring groups and side chains in the enzyme chymotrypsi
222. Chemical modification as a probe of structure and function, Chap
223. Molecular weight, molecular volume, and hydration of proteins in solutio
224. X-ray study of chymotrypsin and hemoglobi
225. Shape and size of dissolved particles from the smallest angle of diffusely diffracted X-ray
226. The molecular size and shape of the pancreatic proteins. I. Sedimentation studies on chymotrypsinogen and on α- and γ-chymotrypsi
227. Essential groups of crystalline chymotrypsi
228. The formation of anhydrochymotrypsin by removing the elements of water from the serine at the active sit
229. Chymotrypsin catalysis. Evidence for a new intermediate. I
230. Inactivation of α-chymotrypsin by a water-soluble carbodiimid
231. Kinetic properties of succinylated and ethylenediamine-amidated δ-chymotrypsi
232. Activity and conformation of the alkaline form of δ-chymotrypsin studied by the specific acylation of isoleucine - 1
233. Chemical derivatives of chymotrypsinogen. I. Reaction with carbon disulfid
234. Chemical derivatives of chymotrypsinogen. II. Reaction with O-methylisoure
235. Reaction of chymotrypsin and chymotrypsin derivatives with benzenediazoniumsulfonate and characterization of the “reactive” histidine of the active cente
236. Cross-linking of α-chymotrypsin and other proteins by reaction with glutaraldehyd
237. Chemical modification of proteins by pyrylium salt
238. Proteins. XXIV. Substitution of e-amino groups of lysine in the molecule of chymotrypsinogen by the reaction with fluorodinitrobenzen
239. The active centre of chymotrypsin. II. Reaction with fluorodinitrobenzen
240. On the elucidation of the pH dependence of chymotrypsin-catalyzed reactions at alkaline p
241. The alkaline pH dependence of chymotrypsin reactions. Postulation of a pH-dependent intramolecular competitive inhibitio
242. The binding of inhibitors to α-chymotrypsin at alkaline p
243. Structure of crystalline α-chymotrypsin. II. A preliminary report including a Hypothesis for the activation mechanis
244. Studies of the activity of chymotrypsi
245. Chymotrypsin, chemical properties and catalysis, Chap
246. Binding of competitive inhibitors to δ-chymotrypsin in the alkaline pH region. Competitive inhibition kinetics and proton-uptake measurement
247. 1 -catalyzed hydrolysis of N-acetyl-L-tryptophan methyl ester (ATME). The involvement of alanine-149 in α-chymotrypsin catalysi
248. The influence of pH on the kinetic constants of α-chymotrypsin-catalyzed esterolysi
249. Two steps in the reaction of chymotrypsin with acetyl-L-phenylalanine ethyl este
250. Sigmoid and bell-shaped pH-rate profiles in α-chymotrypsin-catalyzed hydrolyses. A mechanistic correlatio
251. The responses of three catalytically functional groups in chymotrypsin to changes in acidit
252. Chemical modification by active-site-directed reagents, Chap
253. Methylation of histidine-57 in α-chymotrypsin by methyl p-nitrobenzene-sulfonate. A new approach to enzyme modificatio
254. Catalytic activity of α-chymotrypsin in which histidine-57 has been methylate
255. Structure of crystalline methyl-chymotrypsi
256. Chymotrypsin catalysis in the presence of formaldehyde. pH dependence of ester hydrolysi
257. Chymotrypsinogen: 2.5-A crystal structure, comparison with α-chymotrypsin, and implications for zymogen activatio
258. Three-dimensional structure of tosyl-α-chymotrypsi
259. On the structure and function of bovine tripsinogen and trypsi
260. Comparative structural studies of phosphoglucomutase and chymotrypsi
261. Catalytic properties of carboxymethylchymotrypsin oxidized at the methionine-19
262. Evidence for a functional carboxyl group in trypsin and chymotrypsi
263. The presence of a second conformation-sensitive group at the active center of chymotrypsi
264. p. 195 in published discussion following Neurath, H. and Hartley, B. S., Hydrolysis by chymotrypsi
265. Reaction of tyrosine residues in proteins with carbodiimide reagent
266. Carboxyl group modification in chymotrypsin and chymotrypsinoge
267. A calorimetric study of the chymotrypsinogen family of protein
268. Reactivity of carboxyl groups in chymotrypsinoge
269. On the structural and functional role of carboxylates in chymotrypsinogen
270. S-carboxymethylcysteine from the photolysis of diazoacyl trypsin and chymotrypsi
271. α by dithiothreito
272. Electrolytic reduction of disulfide bonds and biological activity of some protein
273. Identification of the methionine in the active center of ehymotrypsi
274. Modification of a methionine residue near the active site of ehymotrypsi
275. The catalytic activity of methionine-S-(N-2-carboxylisopropyl)carbamyl-methylsulfonium bromide - 192-chymotrypsi
276. Decreased reactivity of organophosphorus inhibitors towards a modified ehymotrypsi
277. The inactivation of α-chymotrypsin with methyl-, trideuteriomethyl-, and trifluoromethyl-substituted N-phenyl-α-bromoacetamide
278. Specific modification of methionine - 192 of α-chymotrypsin by an affinity label exploiting the orienting properties of the linear acetylenic grou
279. Kinetic evidence for the formation of acyl-enzyme intermediates in the α-chymotrypsin-catalyzed hydrolyses of specific substrate
280. The kinetics of α-chymotrypsin reactions in the presence of added nucleophile
281. The kinetics of the α-chymotrypsin-catalyzed hydrolysis and methanolysis of acetyl-L-phenylalanine methyl ester. Evidence for the specific binding of water on the enzyme surfac
282. The influence of pH and deuterium oxide on the kinetics of α-chymotrypsin-catalyzed reaction
283. The reactivity of nucleophilic reagents with furoyl-chymotrypsi
284. Substrate structure effects on the pH dependence of deacylation of acyl-chymotrypsin
285. Orientation effects in reactions of acyl chymotrypsin
286. Pretransition-state protonation and the rate of ehymotrypsin catalysi
287. Chymotrypsin-catalyzed phenyl ester hydrolysis. Evidence for electrophilic assistance on carbonyl oxyge
288. Structure of crystalline α-chymotrypsin. IV. The structure of indoleacryloyl-α-chymotrypsin and its relevance to the hydrolytic mechanism of the enzym
289. The active site in α-chymotrypsin. Absolute configuration and kinetics of hydrolysis of methyl-3,4-dihydroisocoumarin-3-carboxylat
290. Chymotrypsin, Chap
291. Structural changes in the activation of chymotrypsinogen and trypsinogen. Effect of urea on chymotrypsinogen and δ-chymotrypsi
292. Implication of an ionizing group in the control of conformation and activity of chymotrypsi
293. The activation of chymotrypsinogen optical rotation studie
294. Studies of the chymotrypsinogen family. IV. The conversion of chymotrypsinogen A to α-chymotrypsi
295. The conformational transition associated with the activation of chymotrypsinogen to chymotrypsi
296. Activity and conformation of the alkaline form of 6-chymotrypsin studied by the specific acylation of isoleucine-1
297. Three-dimensional structure of tosyl-α-chymotrypsi
298. Structure of crystalline α-chymotrypsin. II. A preliminary report including a hypothesis for the activation mechanis
299. Physicochemical investigation of the chymotrypsins. II. On the mechanism of dimerization of chymotrypsi
300. Sedimentation of chemically modified chymotrypsi
301. Carboxyl terminal groups of proteolytic enzymes. II. Chymotrypsin
302. Dimerization of α-chymotrypsin. I. pH dependence in the acid regio
303. Relation between δ- and α-chymotrypsi
304. Comparison of the π-, δ-, and γ-chymotrypsin family with α-chymotrypsi
305. The acyl-enzyme dimer of chymotrypsi
306. Preliminary x-ray diffraction studies of crystal forms of free and inhibited chymotrypsi
307. Dimerization and activity of chymotrypsin at pH
308. Chemical behavior of charge-transfer complexes. II. Phenanthrene catalysis in acetolysis of 2, 4, 7-trinitro-9-fluorenyl p-toluenesulfonat
309. The effect of charge-transfer complexation on the hydrolysis of some carboxylic acid derivative
310. The stability of some molecular complexes in aqueous mixed solvents. Correlation with solvent surface tensio
311. Secondary valence force catalysis. II. Kinetics of the hydrolysis and aminolysis of carboxylic esters in the presence of micelle-forming detergent
312. Hydrogen bonds between model peptide groups in solutio
313. Chymotrypsin: enzyme concentration and kinetic
314. A chymotrypsin mode
315. Cyclodextrin-imidazole compound
316. Synthesis of monosubstituted cycloamylose
317. Nucleophilic and metal ion acceleration of ester hydrolysis in a hydrophobic complex. A reactive model enzyme syste
318. Macrobicyclic amines. III. Encapsulation of halide ions by in, in-1, (k + 2)-diazabicyclo ‘k · I · m’-alkaneammonium ion
319. Self-ordered polymers and propagative cell-like system
320. Hydrolysis of proteins and dipeptides by ion-exchange resin catalyst
321. Polyvinylsulfonic as a catalyst of hydrolytic reaction
322. Specific effects in acid catalysis by polymeric sulfonic acids in the hydrolysis of the amino ester and related compound
323. Homogeneous hydrolysis of esters with polymer sulfonic acid
324. Specific effects in acid catalysis by ion exchange resins. II. Hydrolysis of esters in water solutio
325. Specific effects in acid catalysis by ion exchange resins. I. Hydrolysis of esters in 70% aqueous aceton
326. Selectivity in solvolyses catalyzed by poly-(4-vinylpyridine
327. The esterolytic catalytic catalysis of poly-4(5)-vinyl-imidazole and poly-5(6)-vinyl-benzimidazol
328. The enhanced esterolytic catalysis of poly-4(5)-vinylimidazole and poly-5(6)-vinylbenzimidazol
329. Selective catalysis of the copolymer of 4(5)-vinylimidazole and acrylic aci
330. The activation parameters for polymeric imidazole catalysis. The efficiency of multifunctional catalysis on a polymer chai
331. Selective catalysis involving reversible association of a synthetic polymeric catalyst and substrat
332. Investigation of a synthetic catalytic system exhibiting substrate selectivity and competitive inhibitio
333. Observation of Michaelis-Menten kinetics in the hydrolysis of a phenyl ester catalyzed by an imidazole-containing polyme
334. Imidazole catalysis in aqueous systems. II. Inhibition studies on the enzymelike catalysis in the hydrolysis of a phenyl ester by an imidazole-containing copolyme
335. Hydrolysis of phenyl ester catalyzed by a hydrophobic imidazole derivative in an aqueous system: an enzyme mode
336. Imidazole catalyses in aqueous solution. IV. Bimolecular and Michaelis-Menten type catalysis of a phenyl ester hydrolysis by some hydrophobic imidazole derivative
337. Imidazole catalyses in aqueous systems. V. The enzyme-like catalysis in the hydrolysis of a phenyl ester by copolymers containing a benzimidazole group. Rate acceleration by bound phenols and the mode of side chain aggregation in polymer catalyst
338. Macromolecule-small molecule interactions: a synthetic macromolecule with high esterolytic activit
339. Enhanced rates due to apolar interactions between polymer and substrat
340. Macromolecule-small molecule interactions: a synthetic polymer with greater affinity than serum albumin for small molecule
341. Macromolecule-small molecule interactions: strong binding and cooperativity in a model synthetic polyme
342. Synthetic derivatives of polyethyleneimine with enzyme-like catalytic activity (synzymes
343. Macromolecule-small molecule interactions. Strong binding by intramolecularly cross-linked polylysin
344. Imidazole catalysis. I. The catalysis of the hydrolysis of phenyl acetates by imidazol
345. Synthetic histidine-containing polypeptides as catalysts for the hydrolysis of p-nitrophenyl acetat
346. The kinetic consequences of intermolecular attraction. I. The aminolysis of p-nitrophenyl decanoate and acetate by n-decylamine and ethylamin
347. Imidazole-catalyzed displacement of an amine from an amide by a neighboring hydroxyl group. A model for the acylation of chymotrypsi
348. Catalysis in dipolar aprotic solvents. A proton-relay mechanism resembling the mechanism of action of serine enzyme
349. Intramolecular catalysi
350. A source for the specific catalytic power of enzymes: Orbital steerin
351. On the concept of orbital steering in catalytic reaction
352. Entropic contributions to rate accelerations in enzymic and intramolecular reactions and the chelate effec
353. Cycloamyloses as catalyst
354. Imidazole catalyses in aqueous systems. VI. The enzyme-like catalysis in the hydrolysis of a phenyl ester by phenylimidazole-containing copolymers. The correlation between binding capacity and catalytic activit