ISSN:
1432-0428
Keywords:
Nonsuppressible insulin-like activity
;
NSILA-carrier protein
;
human serum
;
perfused rat heart
;
glucose uptake
;
hormone binding
Source:
Springer Online Journal Archives 1860-2000
Topics:
Medicine
Notes:
Summary Human serum in a concentration of 10% in the perfusion medium failed to increase glucose uptake by the isolated perfused rat heart, indicating that nonsuppressible insulin-like activity (NSILA) in whole serum was inactive in this system. When NSILA-carrier protein was added to partially purified NSILA-S, its biological activity on the rat heart disappeared. In contrast, the action of insulin was not affected by the presence of NSILA-carrier protein. Binding of125I-labelled NSILA-S to rat heart was inhibited by NSILA-carrier protein.125I-labelled insulin binding was not inhibited. These results support the hypothesis that NSILA-S bound to serum carrier protein is a large molecular compound which does not readily diffuse out of the capillary bed and therefore does not exert insulin-like effects in vivo.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01219425
