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Solubilization of membrane-bound acid alpha-glucosidase by proteolysis.

Abstract：

:The membrane-bound acid alpha-glucosidase was purified partially (400-fold) from human placenta by solubilization with trypsin, concanavalin A-Sepharose chromatography, Ultrogel AcA-34 gel filtration, and Sephadex G-100 affinity chromatography. Two molecular forms of the enzyme were found in the final preparation of the purified enzyme. They were identical in molecular weight with a precursor (110 kDa) and an early intermediate form (105 kDa) of this enzyme. Also direct incubation of the membrane fraction without trypsin resulted in a release mainly of the 105 kDa form, which was inhibited by N-ethylmaleimide, but not by leupeptin, pepstatin or phenylmethylsulfonylfluoride. It was concluded that the precursor of acid alpha-glucosidase is an intrinsic membrane protein, which is transported into lysosomes after solubilization by proteolysis.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Tsuji A,Suzuki Y

doi

10.1016/s0006-291x(88)80512-6

subject

Has Abstract

pub_date

1988-03-30 00:00:00

pages

1358-63

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(88)80512-6

journal_volume

151

pub_type

杂志文章

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