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Volumn 61, Issue 1, 1997, Pages 52-57

Histidine modification of human serum butyrylcholinesterase

Author keywords

[No Author keywords available]

Indexed keywords

CHOLINESTERASE; DIETHYL PYROCARBONATE; HISTIDINE; TOSYLLYSYL CHLOROMETHYL KETONE; TOSYLPHENYLALANYL CHLOROMETHYL KETONE;

EID: 0031171811     PISSN: 10773150     EISSN: None     Source Type: Journal    
DOI: 10.1006/bmme.1997.2578     Document Type: Article
Times cited : (4)

References (15)
  • 3
    • 0027254853 scopus 로고
    • Sheep brain pseudocholinesterase: Inhibition kinetics of the partially purified enzyme by some substrate analogues
    • 3. Çokuǧraş AN, Tezcan EF. Sheep brain pseudocholinesterase: Inhibition kinetics of the partially purified enzyme by some substrate analogues. Chem Biol Interactions 87:259-264, 1993.
    • (1993) Chem Biol Interactions , vol.87 , pp. 259-264
    • Çokuǧraş, A.N.1    Tezcan, E.F.2
  • 4
    • 0011134856 scopus 로고
    • Site specific reagents for chymotrypsin, trypsin and other serine proteases
    • (Hirs CHW, Ed.) New York: Academic Press
    • 4. Shaw E. Site specific reagents for chymotrypsin, trypsin and other serine proteases. In Methods in Enzymology (Hirs CHW, Ed.). New York: Academic Press, 1972, Vol XXV, pp 655-671.
    • (1972) Methods in Enzymology , vol.25 , pp. 655-671
    • Shaw, E.1
  • 5
    • 0014955676 scopus 로고
    • Methylation of histidine-57 in α-chymotrypsin by methyl p-nitrobenzenesulfonate. A new approach to enzyme modification
    • 5. Nakagawa Y, Bender ML. Methylation of histidine-57 in α-chymotrypsin by methyl p-nitrobenzenesulfonate. A new approach to enzyme modification. Biochemistry 9:259-267, 1970.
    • (1970) Biochemistry , vol.9 , pp. 259-267
    • Nakagawa, Y.1    Bender, M.L.2
  • 8
    • 0017862859 scopus 로고
    • Comparison of atypical and usual human serum cholinesterase
    • Purification, number of active sites, substrate affinity and turnover number.
    • 8. Lockridge O, LaDu BN. Comparison of atypical and usual human serum cholinesterase. Purification, number of active sites, substrate affinity and turnover number. J Biol Chem 253:361-366, 1978.
    • (1978) J Biol Chem , vol.253 , pp. 361-366
    • Lockridge, O.1    LaDu, B.N.2
  • 9
    • 0003518480 scopus 로고
    • Toronto: Wiley
    • 9. Segel IH. Enzyme Kinetics. Toronto: Wiley, 1975, pp 125-136.
    • (1975) Enzyme Kinetics , pp. 125-136
    • Segel, I.H.1
  • 10
    • 0003518480 scopus 로고
    • Toronto: Wiley
    • 10. Segel IH. Enzyme Kinetics. Toronto: Wiley, 1975, pp 178-189.
    • (1975) Enzyme Kinetics , pp. 178-189
    • Segel, I.H.1
  • 12
    • 0015104092 scopus 로고
    • Reactivity of His-57 in chymotrypsin to alkylation
    • 12. Shaw E, Ruscica J. Reactivity of His-57 in chymotrypsin to alkylation. Arch Biochem Biophys 145:484-489, 1971.
    • (1971) Arch Biochem Biophys , vol.145 , pp. 484-489
    • Shaw, E.1    Ruscica, J.2
  • 13
    • 0014802965 scopus 로고
    • Subtilisin BPN': Inactivation by chloromethyl ketone derivatives of peptide substrates
    • 13. Morihara K, Oka T. Subtilisin BPN': Inactivation by chloromethyl ketone derivatives of peptide substrates. Arch Biochem Biophys 138:526-531, 1970.
    • (1970) Arch Biochem Biophys , vol.138 , pp. 526-531
    • Morihara, K.1    Oka, T.2
  • 14
    • 0027066990 scopus 로고
    • A computer model of glycosylated human butyryl-cholinesterase
    • 14. Millard CB, Broomfield CA. A computer model of glycosylated human butyryl-cholinesterase. Biochem Biophys Res Commun 189:1280-1286, 1992.
    • (1992) Biochem Biophys Res Commun , vol.189 , pp. 1280-1286
    • Millard, C.B.1    Broomfield, C.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.