6533b835fe1ef96bd129e980
RESEARCH PRODUCT
Two proteases from nuclei of rat testis cells. II. Inhibitors
J.logan IrvinGoffredo CognettiSalvatore Perrierasubject
chemistry.chemical_classificationProteasesProteasemedicine.medical_treatmentSubstrate (chemistry)BiologyTesticleTrypsinMolecular biologyCell nucleusmedicine.anatomical_structureEnzymeBiochemistrychemistrymedicineAnimal Science and ZoologySpermatogenesismedicine.drugdescription
Abstract Proteases Rc and Kc of the nuclei of rat testis cells exhibit considerable differences in susceptibility to various protease inhibitors. Protease Rc is inhibited by D‐phenylalanyl‐L‐propyl‐L‐arginine chlormethylketone and p‐nitrophenyl‐p1‐guanidino ben‐zoate. Protease Kc is inhibited by Nα‐p‐tosyl‐L‐lysine chlormethylketone, N‐p‐tosyl‐phenylalanine chlormethylketone, N‐carbobenzoxy‐L‐phenylalanine chloromethylketone and p‐nitrophenyl‐p'‐guanidino‐benzoate. Neither protease is inhibited by 10 mM phenylmethanesulphonyl‐fluoride or p‐chloromercuri‐benzoate. p‐nitrophenyl‐p1‐guanidino‐benzoate is a substrate for protease Rc with release of p‐nitrophenol, however the protease activity is not restored during a period of 8 hours after removal of excess p‐nitrophenyl‐p1‐guanidino‐benzoate. Both proteases can bind to immobilized soybean trypsin inhibitors.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1987-01-01 | Bollettino di zoologia |