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Titolo:
COMPARISON OF LHRH-PEPTIDASE AND PLASMINOGEN-ACTIVATOR ACTIVITY IN RAT TESTIS EXTRACTS
Autore:
HEDGER MP; CULLER MD;
Indirizzi:
MONASH UNIV,MONASH MED CTR,INST REPROD & DEV CLAYTON VIC 3168 AUSTRALIA BIOMEASURE INC MILFORD MA 01757
Titolo Testata:
Reproduction, fertility and development
fascicolo: 7, volume: 9, anno: 1997,
pagine: 659 - 664
SICI:
1031-3613(1997)9:7<659:COLAPA>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
HORMONE-RELEASING HORMONE; PROLINE CLEAVING ENZYME; ANGIOTENSIN-CONVERTING ENZYME; PROLYL ENDOPEPTIDASE; FOLLICULAR-FLUID; METALLOENDOPEPTIDASE; TISSUES; PURIFICATION; UROKINASE; AGONIST;
Keywords:
GONADOTROPIN-RELEASING HORMONE ASSOCIATED PEPTIDE; ANGIOTENSINS; PROLYL ENDOPEPTIDASE; PLASMIN; PLASMINOGEN ACTIVATOR INHIBITORS;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
43
Recensione:
Indirizzi per estratti:
Citazione:
M.P. Hedger e M.D. Culler, "COMPARISON OF LHRH-PEPTIDASE AND PLASMINOGEN-ACTIVATOR ACTIVITY IN RAT TESTIS EXTRACTS", Reproduction, fertility and development, 9(7), 1997, pp. 659-664

Abstract

Testicular LHRH-peptidase and testicular urokinase-type plasminogen activator are Sertoli cell-secreted proteases which display similar molecular properties. However, there is relatively little information regarding the substrate specificity and potential cross-reactivity of these enzymes. Testicular extracts were prepared from homogenates of whole rat testes and assessed by LHRH-peptidase assay, and by radial caseinolysis assays for plasminogen activator and plasmin-like activity. Following partial purification of the protease activities in testicular extracts by gel filtration and ion-exchange chromatography, it was confirmed that testicular LHRH-peptidase and plasminogen activator are clearly separable. There was no detectable plasmin-like activity in the testicular extracts; however, the extracts were found to contain an inhibitor, or inhibitors, of both plasminogen activator and plasmin activity. In addition to LHRH and Gly(6)-substituted LHRH analogues, the partially purified LHRH-peptidase degraded both angiotensins I and II, but not the gonadotrophin-releasing-hormone-associated peptide derivedfrom the LHRH precursor molecule. These properties of the LHRH-peptidase provide further evidence that it is a testis-specific prolyl endopeptidase, involved in regulating and/or limiting peptide activity in the testis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 11/07/20 alle ore 21:07:10