Thiolation and disulphide cross-linking of insulin to form macromolecules of potential therapeutic value.

Abstract:

:Macromolecules have been prepared containing native insulin carried by a modified insulin skeleton made by partially thiolating the insulin hexamer and forming intermolecular cross-links through disulphide bridges. Oxidation of partially thiolated insulin (0.5-0.7 SH group/mole), formed by reacting insulin with AHTL, with, (a) potassium ferricyanide, (b) Cu++-oxygen gave water soluble macromolecules containing 20-26 and 410-708 monomer units respectively which had rod-random coil shape (light scattering). The larger molecules formed by (b) contained 8g-atom CU++/hexamer unit and insulin. The insulin was firmly bound within the marcomolecules and was probably bound within an insulin-modified insulin hexamer through coordination to copper.

journal_name

Adv Exp Med Biol

authors

Mahbouba M,Smith HJ

doi

10.1007/978-1-4684-3282-4_15

subject

Has Abstract

pub_date

1977-01-01 00:00:00

pages

247-60

eissn

0065-2598

issn

2214-8019

journal_volume

86A

pub_type

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