scholarly journals The subunit structure of the high affinity insulin receptor. Evidence for a disulfide-linked receptor complex in fat cell and liver plasma membranes.

1980 ◽  
Vol 255 (4) ◽  
pp. 1722-1731 ◽  
Author(s):  
P.F. Pilch ◽  
M.P. Czech
Keyword(s):  
Insulin Receptor ◽  
Plasma Membranes ◽  
Subunit Structure ◽  
Receptor Complex ◽  
Fat Cell ◽  
High Affinity ◽  
Liver Plasma Membranes

scholarly journals Quantitative Aspects of the Insulin-Receptor Interaction in Liver Plasma Membranes

1974 ◽  
Vol 249 (7) ◽  
pp. 2249-2257 ◽  
Author(s):  
C. Ronald Kahn ◽  
Pierre Freychet ◽  
Jesse Roth ◽  
David M. Neville
Keyword(s):  
Insulin Receptor ◽  
Plasma Membranes ◽  
Receptor Interaction ◽  
Liver Plasma Membranes

scholarly journals The NSILA-s receptor in liver plasma membranes. Characterization and comparison with the insulin receptor

1975 ◽  
Vol 250 (23) ◽  
pp. 8990-8996 ◽  
Author(s):  
K Megyesi ◽  
CR Kahn ◽  
J Roth ◽  
DM Neville ◽  
SP Nissley ◽  
...  
Keyword(s):  
Insulin Receptor ◽  
Plasma Membranes ◽  
Liver Plasma Membranes

Subunit Structure and Regulation of the Insulin-Receptor Complex

1985 ◽  
pp. 3-29 ◽  
Author(s):  
Jeffrey E. Pessin ◽  
Cristina Mottola ◽  
Kin-Tak Yu ◽  
Michael P. Czech
Keyword(s):  
Insulin Receptor ◽  
Subunit Structure ◽  
Receptor Complex

Demonstration of a high affinity Ca2+-ATPase in rat liver plasma membranes

1982 ◽  
Vol 105 (2) ◽  
pp. 488-494 ◽  
Author(s):  
Yasushi Iwasa ◽  
Takafumi Iwasa ◽  
Kenji Higashi ◽  
Kazuo Matsui ◽  
Eishichi Miyamoto
Keyword(s):  
Rat Liver ◽  
Plasma Membranes ◽  
High Affinity ◽  
Liver Plasma Membranes ◽  
Rat Liver Plasma Membranes

scholarly journals Evidence concerning the mechanism of insulin-receptor interaction and the structure of the insulin receptor from biological properties of covalently linked insulin dimers

1983 ◽  
Vol 216 (3) ◽  
pp. 687-694 ◽  
Author(s):  
M A Tatnell ◽  
R H Jones ◽  
K P Willey ◽  
A Schüttler ◽  
D Brandenburg
Keyword(s):  
Insulin Receptor ◽  
Plasma Membranes ◽  
Gel Filtration ◽  
Biological Properties ◽  
Receptor Interaction ◽  
Cross Linking ◽  
Receptor Complex ◽  
Biological Responses ◽  
Rat Liver Plasma Membranes ◽  
Covalently Linked

Covalently linked insulin dimers have been prepared by cross-linking two insulin monomers with a flexible suberoyl chain at either the B1 phenylalanine or the B29 lysine residue. Binding potencies of dimers determined by inhibition of binding of 125I-insulin to isolated rat liver plasma membranes or adipocytes were 2.5-7-fold greater than their abilities to stimulate lipogenesis in adipocytes. Rates of liver plasma-membrane-associated degradation of labelled insulin and dimers, measured by gel filtration, were similar at 37 degrees C. Binding and lipogenesis potencies of dimers prepared by substitution of each monomeric half of an asymmetrical dimer with desoctapeptide insulin, an almost inactive derivative, implicated the B1-cross-linked monomeric half as predominantly interacting with the insulin receptor. These results suggest that (1) dimers bind univalently to a bivalent insulin-receptor complex, in which the two individual binding subunits are arranged with anti-parallel symmetry and (2) the mechanism by which insulin binds and initiates its biological responses requires a conformational change within the insulin-receptor complex and/or in the insulin molecule for full biological expression.

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