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Proteolytic cleavages in alpha 1-antitrypsin and microheterogeneity.

Abstract：

:Antitrypsin was resolved into two pools by ion-exchange chromatography. Pool 2 contained three anodal isoinhibitors and an N-terminal sequence identical with the one found by others. Pool 1 contained, in addition to the anodal ones two cathodal isoinhibitors as well. The sequencing data of Pool 1 indicate that the cathodal proteins are formed from the anodals by a cleavage of the Gly5-Asp6 bond in the molecule.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Hercz A

doi

10.1016/0006-291x(85)91664-x

subject

Has Abstract

pub_date

1985-04-16 00:00:00

pages

199-203

issue

1

eissn

0006-291X

issn

1090-2104

pii

0006-291X(85)91664-X

journal_volume

128

pub_type

杂志文章

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