[Isolation and study of the properties of an insulin-binding protein from the blood serum].
A question of the existence of blood proteins binding unmodified insulin has remained open for many years. This paper is devoted to the description of a method of isolation and characteristics of the insulin-binding protein (IBP) isolated from rat and human blood sera. The level of IBP in the serum was 0.12-0.15 mg/ml. The protein was referred to IgG basing on the data of electrophoresis under denaturing conditions, immunoelectrophoresis and immunoenzymatic analysis. The constant of protein association with insulin varied with regard to a source within 1.5.10(-7) to 2.5.10(7) M-1. The studied protein bound both 125I-modified and unmodified insulin preparations. The calculation based on IBP parameters, showed that no less than half of the blood insulin must be in a bound condition. The capacity of such insulin-binding system is rather great and is capable of leveling down sharp changes in a blood insulin concentration.
Zhvirblene
A A
AA
Barbashov
S F
SF
Severin
E S
ES
D000818:Animals; D001797:Blood Protein Electrophoresis; D001798:Blood Proteins / Q000302:isolation & purification* / Q000378:metabolism; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007122:Immunoelectrophoresis; D007074:Immunoglobulin G / Q000302:isolation & purification / Q000378:metabolism; D007328:Insulin / Q000097:blood*; D008970:Molecular Weight; D011485:Protein Binding; D051381:Rats
D001798:Blood Proteins; D007074:Immunoglobulin G; D007328:Insulin
Vydelenie i izuchenie svoĭstv insulinsviazyvaiushchego belka syvorotki krovi.