Interfacial catalysis by phospholipase A2: monomeric enzyme is fully catalytically active at the bilayer interface.
Interfacial catalysis by phospholipase A2: monomeric enzyme is fully catalytically active at the bilayer interface.
复制标题
磷脂酶 A2 的界面催化:单体酶在双层界面具有完全催化活性。
DOI:
10.1021/bi00243a038
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发表时间:
1991
期刊:
影响因子:
2.9
通讯作者:
Verheij,HM
中科院分区:
文献类型:
--
作者:
Jain,MK;Ranadive,G;Yu,BZ;Verheij,HM
Materials and Methods All reagents and buffers used in this study were analytical grade. 7V-Methylisatoic anhydride was purchased from Mo-1 Abbreviations: AMPA, pig pancreatic PLA2 in which terminal amino groups of all lysines have been amidinated; An87-PLA2, pig pancreatic PLA2 covalently modified at lysine87 with IV-methylisatoic anhydride; DMPM, l, 2-dimyristoyl-in-glycero-3-phosphomethanol; DMPC, l, 2-dimyristoyI-jvi-giycero-3-phosphocholine; DTPM, 1, 2-ditetradecyl-in-glycero-3-phosphomethanol; DTPC, 1, 2-ditetradecyl-rnglycero-3-phosphocholine; HDNS, dansylated hexadecylphospho-ethanolamine; Me-PLA2, pig pancreatic PLA2 methylated at His-48 by methyl-4-nitrobenzene sulfonate; N „the number of substrate molecules hydrolyzed per enzyme molecule; NOB, 4-nitro-3-octanoyloxy benzoate; NOB-PLA2, pig pancreaticPLA2 to which an octanoyl group has been transferred from NOB; Oct-PLA2, pig pancreatic PLA2 modified at His-48 with 1-bromo-2-octanone; Palm-110 PLA2, pig pancreaticPLA2 with a palmitoyl group at lysine 110; PLA2, phospholipaseA2.