Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P00790 (PGA)
 2,475 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Five pepsinogens were purified from gastric mucosa of Japanese monkey by DEAE-cellulose column chromatography and Sephadex G-100 gel filtration. Each was shown to be homogeneous by polyacrylamide disc gel electrophoresis. They were designated as pepsinogens I, II, III-1, III-2, and III-3, respectively, based on the elution profile on DEAE-cellulose chromatography. The molecular weights of pepsinogens I and II were 48,000 and 43,000, respectively, and those of the other three were 40,000. Each pepsinogen was converted to pepsin [EC 3.4.23.1] by acidification, and some characteristics, e.g. the pH dependence of activity, sensitivity to various inhibitors, stability to alkali, and hydrolytic activity toward N-acetyl-L-phenylalanyl-3,5-diiodo-L-tyrosine (APDT), were determined. The characteristics of pepsins I and II were the same, and those of pepsins III-1, III-2, and III-3 were similar. Pepsin III-3 showed high stability to alkali (pH 8.0), while the others were less stable. Each pepsin hydrolyzed APDT and was inhibited by acid protease-specific inhibitors, e.g. pepstain, diazoacetyl-DL-norleucine methyl ester (DAN), 1,2-epoxy-3-(p-nitrophenoxy)propane (EPNP), and p-bromophenacyl bromide. The compositions of pepsins I and II were the same, indicating that they are the same protein, and those of pepsins III-1, III-2, and III-3 resembled that of human pepsin. The diversity of pepsinogens and pepsins is discussed in comparison with pepsinogens and pepsins from other animals.
 ...
PMID:Pepsinogens and pepsins from gastric mucosa of Japanese Monkey. Purification and characterization. 82 Jun 94

BW-175 is a newly synthesized renin inhibitor which is a nonpeptidic, norleucine analog. Its IC50 values for renin activity in human, squirrel monkey, marmoset, dog, hog, rabbit and rat plasma were 3.3, 6.6, 2.4, 42, 110, 86 and 3500 nM, respectively, and 26 microM for cathepsin D. Pepsin and angiotensin converting enzyme were hardly inhibited at 10(-4) M. BW-175 showed an oral bioavailability of 2.8% at 10 mg/kg and 9.7% at 30 mg/kg in rats. In normotensive, furosemide-treated high-renin marmosets, BW-175 (30 mg/kg p.o.) caused an intensive reduction in plasma renin activity and plasma angiotensin I formation, associated with a reduction in systolic blood pressure of 10-20 mm Hg for 2 hours.
 ...
PMID:A novel nonpeptidic, orally active renin inhibitor. 249 4

An acid proteinase of Dirofilaria immitis worms was purified 437-fold by gel filtration on Sephadex G-75 followed by pepstatin-Agarose gel affinity chromatography. The enzyme with a molecular weight of 42 kDa was homogeneous as judged by both affinity chromatography and SDS-polyacrylamide gel electrophoresis. Polyacrylamide disc electrophoresis at pH 8.9, however, revealed that the enzyme was composed of five multi-forms, all carrying proteinase activity. Optimum pH of the enzyme was in the range of pH 2.8 to 3.4, and its isoelectric point ranged between 5.8 and 6.4. The purified proteinase showed a potent activity against hemoglobin and myoglobin releasing acid soluble peptides, but not free amino acids. When enzymatic properties of the proteinase was compared with mammalian cathepsin D and pepsin, D. immitis proteinase activity was reduced to about 80% of the initial activity by incubating at neutral pH and 50 degrees C for 5 min, just like cathepsin D, which remained intact. Pepsin activity was completely destroyed under the same condition. An aspartic proteinase inhibitor, 1,2-epoxy-3-(p-nitrophenoxy)propane, which inhibited pepsin by 30% at 37 degrees C for 10 min, did show little effects on D. immitis proteinase and cathepsin D. Inhibitory effect of diazoacetyl-DL-norleucine methyl ester (DAN) on D. immitis proteinase was intermediate (50% after 60 min). Immunolocalization of the proteinase in the worm tissue using its monoclonal antibodies revealed that the enzyme was localized in the intestine as well as uterine wall and some small granules of microfilariae in the uterus.
 ...
PMID:Purification and characterization of an acid proteinase from Dirofilaria immitis worms. 854 Mar 32