从大鼠肺中溶解胰岛淀粉样多肽（IAPP）和降钙素基因相关肽（CGRP）的结合位点。

Solubilization of binding sites for IAPP and CGRP from rat lung.

作者信息

Bhogal R, Smith D M, Bloom S R

机构信息

Department of Medicine, Royal Postgraduate Medical School, Hammersmith Hospital, London, UK.

出版信息

Peptides. 1994;15(8):1383-90. doi: 10.1016/0196-9781(94)90113-9.

DOI:10.1016/0196-9781(94)90113-9

PMID:7700841

Abstract

Functional binding sites for [125I]IAPP and [125I]CGRP were solubilized from rat lung membranes with CHAPSO (10 mM). Rat IAPP had a higher affinity (Ki = 22.9 nM) for [125I]IAPP binding and rat alpha CGRP (Ki = 0.904 nM) had a higher affinity for [125I]CGRP binding over related peptides. [125I]IAPP binding was unaffected by GTP gamma S, but [125I]CGRP binding was 50% inhibited, indicating solubilization of a G-protein-receptor complex for CGRP but not IAPP binding. Wheat germ agglutinin affinity columns gave a 25-fold purification of IAPP binding sites, but no CGRP binding sites were eluted from the column, indicating different patterns of glycosylation of the two sites.

摘要

用CHAPSO（10 mM）从大鼠肺膜中溶解[125I]胰岛淀粉样多肽（IAPP）和[125I]降钙素基因相关肽（CGRP）的功能性结合位点。大鼠IAPP对[125I]IAPP结合具有更高的亲和力（Ki = 22.9 nM），而大鼠αCGRP（Ki = 0.904 nM）对[125I]CGRP结合的亲和力高于相关肽。[125I]IAPP结合不受GTPγS影响，但[125I]CGRP结合受到50%抑制，表明溶解出了CGRP而非IAPP结合的G蛋白受体复合物。麦胚凝集素亲和柱对IAPP结合位点进行了25倍的纯化，但未从柱上洗脱到CGRP结合位点，表明这两个位点的糖基化模式不同。