Actions of Anti-insulin Serum on the Interactions of Insulin with Human Liver Membranes
-
- Sasaki Takashi
- The Second Department of Medicine, Hokkaido University School of Medicine
-
- Komori Katsutoshi
- The Second Department of Medicine, Hokkaido University School of Medicine
-
- Nakayama Hidetaka
- The Second Department of Medicine, Hokkaido University School of Medicine
-
- Nakagawa Shoichi
- The Second Department of Medicine, Hokkaido University School of Medicine
Bibliographic Information
- Other Title
-
- ヒト肝細胞膜のインスリン結合に及ぼすインスリン抗体の作用
- ヒト カン サイボウ マク ノ インスリン ケツゴウ ニ オヨボス インスリン
Search this article
Description
The actions of porcine insulin antiserum on the interactions of insulin with human liver membranes were investigated. When 125I-insulin was preincubated with anti-insulin serum, the insulin binding was decreased in relation to the concentration of antiserum. The 125I-insulin binding to liver membranes in the presence of serum from insulin-treated patients, had an inverse relationship with the 125I-insulin binding to patient serum (r=0.93, p<0.05).<BR>Scatchard plot analysis of the 125I-insulin binding data revealed no change in affinity in the binding data in the presence of antiinsulin serum, but there was a decrease in total binding capacity (high affinity plus low affinity). Anti-insulin serum accelerated the dissociation of insulin from liver membranes as compared to the control (p<0.05), and 98.5% of the dissociated insulin was found to rebind to anti-insulin serum. Similarly, 125I-insulin dissociated from anti-insulin serum rebound to liver membranes.<BR>The above results suggest that in vivo insulin bound to insulin antibodies does not bind to insulin receptor, and that insulin antibodies accelerate the dissociation of insulin from the receptor.
Journal
-
- Journal of the Japan Diabetes Society
-
Journal of the Japan Diabetes Society 24 (4), 487-492, 1981
THE JAPAN DIABETES SOCIETY
- Tweet
Details 詳細情報について
-
- CRID
- 1390282679885638912
-
- NII Article ID
- 130004336930
-
- NII Book ID
- AN00166576
-
- ISSN
- 1881588X
- 0021437X
-
- NDL BIB ID
- 2349492
-
- Data Source
-
- JaLC
- NDL
- CiNii Articles
-
- Abstract License Flag
- Disallowed