Heterogeneity of cholecystokinin receptors in pancreas.
Heterogeneity of cholecystokinin receptors in pancreas.
复制标题
胰腺中胆囊收缩素受体的异质性。
DOI：
10.1016/0006-291x(87)91419-7
复制
发表时间：
1987
影响因子：
3.1
通讯作者：
Rosenzweig,SA
中科院分区：
文献类型：
--
作者：
Madison,LD;Jamieson,JD;Rosenzweig,SA
用SH，NH 2异双功能交联剂-马来酰亚胺苯甲酰基N-羟基琥珀酰亚胺酯（MBS），用125 I-CCK-33亲和标记大鼠胰腺质膜、胰腺腺泡细胞和腺泡细胞瘤膜上的胆囊收缩素（CCK）受体，获得了Mr 85 -95 K蛋白的特异性标记。内切糖苷酶F（endo F）在凝胶切片中对该物种的消化表明，至少存在两种含有N-连接聚糖的组分。较小的Mr-85 K蛋白被内切F酶切后生成最终产物Mr-62 K，而较大的Mr-95 K蛋白则生成Mr-55 K和Mr-43 K两种内切F产物。这些发现表明，胰腺腺泡细胞上的CCK受体表现出寡聚体结构，具有两个不同的CCK结合蛋白。
Specific labeling of a major Mr85–95 K protein was obtained using the SH, NH2heterobifunctional cross-linkerm-maleimidobenzoylN-hydroxysuccinimide ester (MBS) to affinity label cholecystokinin (CCK) receptors on rat pancreatic plasma membranes, pancreatic acinar cells and acinar cell tumor membranes with125I-CCK-33. Endoglycosidase F (endo F) digestion of this species in gel slices indicated that at least two components were present which contain N-linked glycans. The smaller protein of Mr∼85 K was digested by endo F to a final product of ∼Mr62 K while the larger Mr∼95 K protein generated two endo F products of Mr55 K and Mr43 K. These findings suggest that the receptor for CCK on pancreatic acinar cells exhibits an oligomeric structure, possessing two distinct CCK-binding proteins.