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豚鼠离体组织中胆囊收缩素26 - 33的C端和N端片段的构效关系研究

Structure-activity studies of C- and N-terminal fragments of cholecystokinin 26-33 in guinea pig isolated tissues.

作者信息

Gaudreau P, St-Pierre S, Pert C B, Quirion R

机构信息

Laboratory of Neuroendocrinology, Notre-Dame Hospital Research Center, Montreal, Quebec, Canada.

出版信息

Neuropeptides. 1987 Jul;10(1):9-18. doi: 10.1016/0143-4179(87)90084-9.

Abstract

In vitro structure-activity studies with cholecystokinin (CCK)/gastrin-related peptides, including C- and N-terminal fragments of CCK 26-33, were undertaken in guinea pig gallbladder and ileum. The general order of potency in both smooth muscle preparations is CCK 26-33 greater than CCK 1-33 greater than 27-33 much much greater than nonsulfated (NS) CCK 26-33 greater than pentagastrin greater than CCK 30-33. None of the CCK fragments exhibit antagonistic properties such as in guinea pig, rat and mouse pancreatic acinar cells and hog duodenum. These observations suggest the existence of CCK receptor sub-types in peripheral tissues.

摘要

利用胆囊收缩素(CCK)/胃泌素相关肽进行了体外结构-活性研究,包括CCK 26-33的C端和N端片段,研究在豚鼠胆囊和回肠中进行。在两种平滑肌制剂中,效力的一般顺序为CCK 26-33大于CCK 1-33大于27-33远大于非硫酸化(NS)CCK 26-33大于五肽胃泌素大于CCK 30-33。CCK片段在豚鼠、大鼠和小鼠胰腺腺泡细胞以及猪十二指肠中均未表现出拮抗特性。这些观察结果表明外周组织中存在CCK受体亚型。

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