Relationship between protease activity and a sialoglycopeptide inhibitor isolated from bovine brain.

Abstract:

:We have recently described the isolation and purification to homogeneity of a new sialoglycopeptide from bovine brain cell surfaces that reversibly inhibits protein synthesis and DNA synthesis of normal but not transformed cells. Active inhibitory preparations, however, were shown to contain a protease activity that was not lost upon purification. Several experiments were performed to establish the relationship between the proteolytic activity of the sialoglycopeptide and the biological inhibitory activity. Both the protease activity and inhibitory activity were stable at pH 6-8 but were reduced or completely destroyed below pH 4 and above pH 9. Acid inactivation was reversible and upon dialysis, both the biological inhibitory and protease activities were regained. Deglycosylation and CNBr cleavage indicated that the polypeptide backbone, rather than carbohydrate moiety, played an important role in the protease and biological inhibitory activities. Furthermore, chemical modification of amino and tyrosine groups indicated that both residues are essential for both activities. Thus, the biological inhibitory activity and protease activity are very closely related and most likely reside with the same polypeptide sequence.

journal_name

J Cell Biochem

authors

Sharifi BG,Bascom CC,Fattaey H,Nash S,Johnson TC

doi

10.1002/jcb.240310106

subject

Has Abstract

pub_date

1986-01-01 00:00:00

pages

41-57

issue

1

eissn

0730-2312

issn

1097-4644

journal_volume

31

pub_type

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