Localisation of a particulate luliberin hydrolysing activity in microsomal membranes of guinea pig brain
Author:
Publisher
Elsevier BV
Subject
Cellular and Molecular Neuroscience,Clinical Biochemistry,Endocrinology,Physiology,Biochemistry
Reference34 articles.
1. An evaluation of the role of pyroglutamyl peptidase, a postproline cleaving enzyme and a postproline dipeptidyl aminopeptidase, each purified from the soluble fraction of guinea-pig brain on the degradation of thyroliberin in vitro;Browne;Eur. J. Biochem.,1983
2. Catabolism of thyroliberin by rat adenohypophyseal tissue extracts;Bauer;Eur. J. Biochem.,1980
3. Catabolism of neuropeptides by a brain proline endopeptidase;Taylor;Biochem. Biophys. Res. Commun.,1980
4. Chymotrypsic-like hydrolysis of luliberin by an adenohypophyseal enzyme of high molecular weight;Horsthemke;Biochem. Biophys. Res. Commun.,1981
5. Cation sensitive neutral endopeptidase: isolation and specificity of the bovine pituitary enzyme;Wilk;J. Neurochem.,1980
Cited by 3 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Subcellular distribution of dipeptidyl aminopeptidase activity against Lys-Ala-NH-Mec in guinea-pig brain;Biochemical Society Transactions;1991-02-01
2. Thyroliberin and luliberin degradation by enzymes in cultured cells of neural origin;Biochemical Society Transactions;1991-02-01
3. Degradation of Thyrotropin-Releasing Hormone and Luteinising Hormone-Releasing Hormone by Enzymes of Brain Tissue;Journal of Neurochemistry;1990-01
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