Purification and immunochemical interrelationship of insulin receptors from rat brain and liver.
Insulin receptors from rat brain and liver were purified. Brain purified receptor exhibited protein bands of apparent Mr = 135,000 and 95,000 molecular weight corresponding to alpha- and beta-subunits, retained a tyrosine specific protein kinase activity and demonstrated phosphorylation that is hormonally sensitive. Antisera were raised against both insulin receptor preparations and enzyme-linked immunosorbent assay was developed. The comparison of two insulin receptors was based on a displacement enzyme-linked immunosorbent assay where antisera were interchanged on predetermined optimal dilutions. This indicated that both insulin receptors possess some unique antigenic determinants thereby implying a structural difference.
Azam
M
M
School of Life Sciences, Jawaharlal Nehru University, New Delhi, India.
Gupta
G
G
Baquer
N Z
NZ
D000818:Animals; D015153:Blotting, Western; D001923:Brain Chemistry; D003429:Cross Reactions; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes; D008099:Liver / Q000737:chemistry*; D008297:Male; D008970:Molecular Weight; D010766:Phosphorylation; D011505:Protein-Tyrosine Kinases / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D011972:Receptor, Insulin / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism; D013552:Swine
D000939:Epitopes; D011505:Protein-Tyrosine Kinases; D011972:Receptor, Insulin