Cathepsin M: a lysosomal proteinase with aldolase-inactivating activity.

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作者信息

Pontremoli S, Melloni E, Salamino F, Sparatore B, Michetti M, Horecker B L

出版信息

Arch Biochem Biophys. 1982 Mar;214(1):376-85. doi: 10.1016/0003-9861(82)90042-x.

DOI:10.1016/0003-9861(82)90042-x

PMID:6282224

Abstract

摘要

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Cathepsin M: a lysosomal proteinase with aldolase-inactivating activity.

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Interaction of rabbit liver cathepsin M and fructose 1,6-bisphosphatase converting enzyme with their endogenous inhibitors.兔肝脏组织蛋白酶M和果糖1,6 -二磷酸酶转换酶与其内源性抑制剂的相互作用。

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Inactivation of fructose 1,6-bisphosphatase by a lysosomal proteinase is reversed by cystamine.半胱胺可逆转溶酶体蛋白酶对1,6-二磷酸果糖酶的失活作用。

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Inactivation of rabbit liver and muscle aldolases by limited proteolysis by lysosomal cathepsin M.溶酶体组织蛋白酶M通过有限的蛋白水解作用使兔肝脏和肌肉醛缩酶失活。

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Sites of cleavage of rabbit muscle aldolase by purified cathepsin M from rabbit liver.兔肝脏中纯化的组织蛋白酶M对兔肌肉醛缩酶的裂解位点。

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Modification of rat liver fructose biphosphate aldolase by lysosomal proteinases.溶酶体蛋白酶对大鼠肝脏果糖二磷酸醛缩酶的修饰作用。

Adv Enzyme Regul. 1982;20:337-50. doi: 10.1016/0065-2571(82)90024-3.

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Endogenous inhibitors of lysosomal proteinases.溶酶体蛋白酶的内源性抑制剂。

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Identification of intracellular degradation intermediates of aldolase B by antiserum to the denatured enzyme.用抗变性醛缩酶B血清鉴定醛缩酶B的细胞内降解中间体

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Characterization of human fructose-1,6-bisphosphatase in control and deficient tissues.

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