-
1
-
-
0014364651
-
Protein denaturation
-
Tanford C. Protein denaturation. Adv. Protein Chem. 23:1968;122-281.
-
(1968)
Adv. Protein Chem.
, vol.23
, pp. 122-281
-
-
Tanford, C.1
-
2
-
-
0018588511
-
Stability of proteins. Small globular proteins
-
Privalov P.L. Stability of proteins. Small globular proteins. Adv. Protein Chem. 33:1979;167-254.
-
(1979)
Adv. Protein Chem.
, vol.33
, pp. 167-254
-
-
Privalov, P.L.1
-
3
-
-
0034902295
-
Folding/unfolding/refolding of proteins: Present methodologies in comparison with capillary zone electrophoresis
-
Righetti P.G., Verzola D. Folding/unfolding/refolding of proteins: present methodologies in comparison with capillary zone electrophoresis. Electrophoresis. 22:2001;2237-2359.
-
(2001)
Electrophoresis
, vol.22
, pp. 2237-2359
-
-
Righetti, P.G.1
Verzola, D.2
-
4
-
-
0008632485
-
Proteolytic enzymes
-
H. Neurath, & K. Bailey. NY: Academic Press
-
Green N.M., Neurath H. Proteolytic enzymes. Neurath H., Bailey K. The proteins. vol. II, part B:1954;1057-1198 Academic Press, NY.
-
(1954)
The proteins
, vol.2
, Issue.PART B
, pp. 1057-1198
-
-
Green, N.M.1
Neurath, H.2
-
5
-
-
0013457640
-
Susceptibility to attack by proteolytic enzymes
-
Hirs C.H.W. NY: Academic Press
-
Rupley I.A. Susceptibility to attack by proteolytic enzymes. Hirs C.H.W. Methods in enzymology. vol. XI:1967;905-917 Academic Press, NY.
-
(1967)
Methods in enzymology
, vol.11
, pp. 905-917
-
-
Rupley, I.A.1
-
6
-
-
0000352442
-
Proteinases as probes of conformation of soluble proteins
-
R.J. Beynon, & J.S. Bond. Oxford: IRL press
-
Price N.C., Johnson C.M. Proteinases as probes of conformation of soluble proteins. Beynon R.J., Bond J.S. Proteolytic enzymes, a practical approach. 1989;163-180 IRL press, Oxford.
-
(1989)
Proteolytic enzymes, a practical approach
, pp. 163-180
-
-
Price, N.C.1
Johnson, C.M.2
-
7
-
-
0028836042
-
Inactivation during denaturation of ribonuclease A in guanidinium chloride is accompanied by unfolding of the active site
-
Yang H.J., Tsou Ch.L. Inactivation during denaturation of ribonuclease A in guanidinium chloride is accompanied by unfolding of the active site. Biochem. J. 305:1995;379-384.
-
(1995)
Biochem. J.
, vol.305
, pp. 379-384
-
-
Yang, H.J.1
Tsou, Ch.L.2
-
9
-
-
0017061233
-
Study of the native-denatured transition in lysozyme: II. Kinetic analysis of protease digestion
-
Imoto T., Fukuda K., Yagishita K. Study of the native-denatured transition in lysozyme: II. Kinetic analysis of protease digestion. J. Biochem. 80:1976;1313-1318.
-
(1976)
J. Biochem.
, vol.80
, pp. 1313-1318
-
-
Imoto, T.1
Fukuda, K.2
Yagishita, K.3
-
10
-
-
0015521749
-
Study of the thermal denaturation mechanism of hen egg-white lysozyme through proteolytic degradation
-
Matthyssens G.E., Simons G., Kanarek L. Study of the thermal denaturation mechanism of hen egg-white lysozyme through proteolytic degradation. Eur. J. Biochem. 26:1972;449-454.
-
(1972)
Eur. J. Biochem.
, vol.26
, pp. 449-454
-
-
Matthyssens, G.E.1
Simons, G.2
Kanarek, L.3
-
11
-
-
0142073622
-
Kinetics of the co-operative proteolysis
-
Vaintraub I.A. Kinetics of the co-operative proteolysis. Nahrung. 42:1998;59-60.
-
(1998)
Nahrung
, vol.42
, pp. 59-60
-
-
Vaintraub, I.A.1
-
12
-
-
0025861347
-
Action of trypsin on glycinin: Mixed-type proteolysis and its kinetics molecular mass of glycinin-T
-
Shutov A.D., Pineda J., Senyuk V.I., Reva V.A., Vaintraub I.A. Action of trypsin on glycinin: mixed-type proteolysis and its kinetics molecular mass of glycinin-T. Eur. J. Biochem. 199:1991;539-543.
-
(1991)
Eur. J. Biochem.
, vol.199
, pp. 539-543
-
-
Shutov, A.D.1
Pineda, J.2
Senyuk, V.I.3
Reva, V.A.4
Vaintraub, I.A.5
-
13
-
-
0017019007
-
Major proteins of soybean seeds. A straightforward fractionation and their characterization
-
Thanh V.H., Shibasaki K. Major proteins of soybean seeds. A straightforward fractionation and their characterization. J. Agric. Food Chem. 26:1976;1117-1121.
-
(1976)
J. Agric. Food Chem.
, vol.26
, pp. 1117-1121
-
-
Thanh, V.H.1
Shibasaki, K.2
-
16
-
-
0001194371
-
Proteolysis of Kunitz soybean trypsin inhibitor Influence on its activity
-
Vaintraub I.A., Yattara H.B. Proteolysis of Kunitz soybean trypsin inhibitor Influence on its activity. J. Agric. Food Chem. 43:1995;862-866.
-
(1995)
J. Agric. Food Chem.
, vol.43
, pp. 862-866
-
-
Vaintraub, I.A.1
Yattara, H.B.2
-
17
-
-
0000405849
-
Difference spectroscopy
-
Hirs C.H.W. NY: Academic Press
-
Herskovits T.T. Difference spectroscopy. Hirs C.H.W. Methods in enzymology. vol. XI:1967;748-775 Academic Press, NY.
-
(1967)
Methods in enzymology
, vol.11
, pp. 748-775
-
-
Herskovits, T.T.1
-
18
-
-
0039791241
-
A study of factors influencing the reactivation of reduced egg white lysozyme
-
Epstein C.J., Goldberger R.F. A study of factors influencing the reactivation of reduced egg white lysozyme. J. Biol. Chem. 238:1963;1380-1383.
-
(1963)
J. Biol. Chem.
, vol.238
, pp. 1380-1383
-
-
Epstein, C.J.1
Goldberger, R.F.2
-
19
-
-
0041643782
-
Cold-insoluble fraction of the water extractable soybean proteins: II. Factors influencing conformational changes in the 11S component
-
Wolf W.I., Briggs D.R. Cold-insoluble fraction of the water extractable soybean proteins: II. Factors influencing conformational changes in the 11S component. Arch. Biochem. Biophys. 76:1958;377-393.
-
(1958)
Arch. Biochem. Biophys.
, vol.76
, pp. 377-393
-
-
Wolf, W.I.1
Briggs, D.R.2
-
21
-
-
0343012481
-
Conformational changes in proteins
-
M.N. Jones. Amsterdam, NY: Elsevier science. Russian translation
-
Pfeil W., Privalov P.L. Conformational changes in proteins. Jones M.N. Biochemical thermodynamics. 1979;95-139 Elsevier science, Amsterdam, NY. Russian translation.
-
(1979)
Biochemical thermodynamics
, pp. 95-139
-
-
Pfeil, W.1
Privalov, P.L.2
-
22
-
-
0014962518
-
Denaturation of globular proteins: II. The interaction of urea with lysozyme
-
Warren J.R., Gordon J.A. Denaturation of globular proteins: II. The interaction of urea with lysozyme. J. Biol. Chem. 245:1970;4097-4104.
-
(1970)
J. Biol. Chem.
, vol.245
, pp. 4097-4104
-
-
Warren, J.R.1
Gordon, J.A.2
-
23
-
-
0016292941
-
Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, α-chymotrypsin and β-lactoglobulin
-
Greene R.F. Jr., Pace C.N. Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, α-chymotrypsin and β-lactoglobulin. J. Biol. Chem. 249:1974;5388-5393.
-
(1974)
J. Biol. Chem.
, vol.249
, pp. 5388-5393
-
-
Greene R.F., Jr.1
Pace, C.N.2
-
24
-
-
0019324834
-
Kinetic study of protein unfolding and refolding using urea gradient electrophoresis
-
Creighton T.E. Kinetic study of protein unfolding and refolding using urea gradient electrophoresis. J. Mol. Biol. 137:1980;61-80.
-
(1980)
J. Mol. Biol.
, vol.137
, pp. 61-80
-
-
Creighton, T.E.1
-
25
-
-
0027478269
-
Analysis of thermal induced protein folding/refolding transitions using free solution capillary electrophoresis
-
Hilser V.J., Worosila G.D., Freire E. Analysis of thermal induced protein folding/refolding transitions using free solution capillary electrophoresis. Anal. Biochem. 208:1993;125-131.
-
(1993)
Anal. Biochem.
, vol.208
, pp. 125-131
-
-
Hilser, V.J.1
Worosila, G.D.2
Freire, E.3
-
26
-
-
0010497165
-
Preliminary investigation of the behavior of lysozyme in urea solutions
-
Léonis J. Preliminary investigation of the behavior of lysozyme in urea solutions. Arch. Biochem. Biophys. 65:1956;182-193.
-
(1956)
Arch. Biochem. Biophys.
, vol.65
, pp. 182-193
-
-
Léonis, J.1
-
27
-
-
0011171506
-
Decrease of glycinin digestibility in excess denaturation; Effect of refolding
-
Kamata Y., Okubo K., Shibasaki K. Decrease of glycinin digestibility in excess denaturation; effect of refolding. Agric. Biol. Chem. 43:1979;1219-1223.
-
(1979)
Agric. Biol. Chem.
, vol.43
, pp. 1219-1223
-
-
Kamata, Y.1
Okubo, K.2
Shibasaki, K.3
-
28
-
-
0015888586
-
Extended conformations of peptides and proteins in urea and guanidine hydrochloride
-
Tiffany M.L., Krimm S. Extended conformations of peptides and proteins in urea and guanidine hydrochloride. Biopolymers. 12:1973;575-587.
-
(1973)
Biopolymers
, vol.12
, pp. 575-587
-
-
Tiffany, M.L.1
Krimm, S.2
-
29
-
-
0142105252
-
Some properties of crystalline papain: Stability toward heat, pH and urea; PH optimum with casein as substrate
-
Lineweaver H., Schwimmer S. Some properties of crystalline papain: stability toward heat, pH and urea; pH optimum with casein as substrate. Enzymologia. 10:1941;81-93.
-
(1941)
Enzymologia
, vol.10
, pp. 81-93
-
-
Lineweaver, H.1
Schwimmer, S.2
-
30
-
-
0142137018
-
The effect of urea and guanidine hydrochloride on activity and optical rotation of crystalline papain
-
Hill R.L., Schwartz H.C., Smith E.L. The effect of urea and guanidine hydrochloride on activity and optical rotation of crystalline papain. J. Biol. Chem. 234:1959;557-572.
-
(1959)
J. Biol. Chem.
, vol.234
, pp. 557-572
-
-
Hill, R.L.1
Schwartz, H.C.2
Smith, E.L.3
|