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Myelin‐Associated Calpain II
Author(s) -
Yanagisawa Katsuhiko,
Sato Shuzo,
O'Shannessy Daniel J.,
Quarles Richard H.,
Suzuki Koichi,
Miyatake Tadashi
Publication year - 1988
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1988.tb01815.x
Subject(s) - myelin , calpain , myelin sheath , neuroscience , chemistry , biology , biochemistry , central nervous system , enzyme
Anti‐chicken muscle calpain (calcium‐activated neutral protease) antibody (ACAb) was found to be absorbed by purified human brain myelin when titrated by enzyme‐linked immunosorbent assay, suggesting the close association of the protease with myelin. To confirm this, calcium‐dependent protease was extracted from myelin membrane and purified on a phenyl Sepharose CL 4B column. It was activated by calcium ion in the millimolar range, and therefore was determined to be calpain II. This enzyme fraction was electrophoresed and immunostained with ACAb, resulting in staining as a single band with apparent molecular weight of 80K. This protease degraded exogenous myelin‐associated glycoprotein. From the present results, it is suggested that calpain is bound to myelin membrane and involved in the turnover of myelin proteins.