Characterization of an enzyme that is capable of processing pro-gonadotropin-releasing hormone protein
- 1 December 1986
- journal article
- research article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 251 (2) , 543-550
- https://doi.org/10.1016/0003-9861(86)90362-0
Abstract
No abstract availableThis publication has 27 references indexed in Scilit:
- Characterization of cDNA for precursor of human luteinizing hormone releasing hormoneNature, 1984
- Processing of Proenkephalin Is Tissue-SpecificScience, 1984
- A novel protease from yeast with specificity towards paired basic residuesNature, 1984
- Processing of normal and non-glycosylated forms of toad pro-opiocortin by rat intermediate (pituitary) lobe pro-opiocortin converting enzyme activityLife Sciences, 1982
- Proopiocortin-Converting Enzyme Activity in Bovine Neurosecretory GranulesEndocrinology, 1982
- A unique proenkephalin-converting enzyme purified from bovine adrenal chromaffin granulesBiochemical and Biophysical Research Communications, 1982
- A “trypsin-like” enzyme in adrenal chromaffin granules: A proenkephalin processing enzymeBiochemical and Biophysical Research Communications, 1982
- An enkephalin-generating enzyme in bovine adrenal medullaBiochemical and Biophysical Research Communications, 1982
- Characterization of proinsulin- and proglucagon-converting activities in isolated islet secretory granules.The Journal of cell biology, 1981
- Enzymic processing of proparathyroid hormone by cell-free extracts of parathyroid glandsBiochemistry, 1977