Relationship Between Isoelectric Point of Native and Chemically Modified Insulin and Liposomal Fusion

Overview

Journal Biochem J

Specialty Biochemistry

Date 1989 Nov 15

PMID 2690824

Citations 1

Authors

R N Farias

A E Lopez Vinals

E Posse

R D Morero

Affiliations

Soon will be listed here.

Abstract

Native insulin causes fusion of negatively charged liposomes in the pH range from 3.0 to 5.5. In marked contrast, insulin with all three amino groups succinylated did not show fusion ability at any pH. On the other hand, insulin amidated with glycine methyl ester with all six carboxyl groups blocked shifted its activity to higher pH, showing a pH range of activity from 3.0 to 7.4. When the carboxyl groups were recovered by hydrolysis of methoxyl groups from glycine methyl ester-treated insulin, the protein obtained (glycyl-insulin with six free carboxyl groups) behaved as native insulin. A good correlation between the isoelectric point values of insulin and its derivatives and their fusion properties was found.

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