Matches in SemOpenAlex for { <https://semopenalex.org/work/W1586150986> ?p ?o ?g. }
Showing items 1 to 79 of
79
with 100 items per page.
- W1586150986 endingPage "1388" @default.
- W1586150986 startingPage "1382" @default.
- W1586150986 abstract "A novel carbonic anhydrase was purified from human saliva with inhibitor affinity chromatography followed by ion-exchange chromatography. The molecular weight was determined to be 42,000 on sodium dodecyl sulfate polyacrylamide gel electrophoresis, indicating that the human salivary enzyme is larger than the cytosolic isoenzymes CA I, CA II, and CA III (Mr 29,000) from human tissue sources. Each molecule of the salivary enzyme had two N-linked oligosaccharide chains which were cleaved by endo-beta-N-acetylglucosaminidase F but not by endo-beta-N-acetylglucosaminidase H, indicating that the oligosaccharides are complex type. The isoelectric point was determined to be 6.4, but significant charge heterogeneity was found in different preparations. The human salivary isozyme has lower specific activity than the rat salivary isozyme and the human red blood cell isozyme II in the CO2 hydratase reaction. The inhibitory properties of the salivary isozyme resemble those of CA II with iodide, sulfanilamide, and bromopyruvic acid, but the salivary enzyme is less sensitive to acetazolamide and methazolamide than CA II. Antiserum raised in a rabbit against the salivary enzyme cross-reacted with CA II from human erythrocytes, indicating that human salivary carbonic anhydrase and CA II must share at least one antigenic site. CA I and CA III did not crossreact with this antiserum. The amount of salivary carbonic anhydrase in the saliva of the CA II-deficient patients was greatly reduced, indicating that the CA II deficiency mutation directly or indirectly affects the expression of the salivary carbonic anhydrase isozyme. From these results we conclude that the salivary carbonic anhydrase is immunologically and genetically related to CA II, but that it is a novel and distinct isozyme which we tentatively designate CA VI." @default.
- W1586150986 created "2016-06-24" @default.
- W1586150986 creator A5035727388 @default.
- W1586150986 creator A5037444081 @default.
- W1586150986 date "1987-01-01" @default.
- W1586150986 modified "2023-10-12" @default.
- W1586150986 title "Purification and characterization of human salivary carbonic anhydrase." @default.
- W1586150986 cites W1484418190 @default.
- W1586150986 cites W1565799270 @default.
- W1586150986 cites W1775749144 @default.
- W1586150986 cites W1969283110 @default.
- W1586150986 cites W1970259861 @default.
- W1586150986 cites W1973164496 @default.
- W1586150986 cites W1973225699 @default.
- W1586150986 cites W1981411420 @default.
- W1586150986 cites W1996499484 @default.
- W1586150986 cites W2002398620 @default.
- W1586150986 cites W2006796622 @default.
- W1586150986 cites W2015369153 @default.
- W1586150986 cites W2045280804 @default.
- W1586150986 cites W2054682108 @default.
- W1586150986 cites W2076387319 @default.
- W1586150986 cites W2087864300 @default.
- W1586150986 cites W2093685361 @default.
- W1586150986 cites W2100837269 @default.
- W1586150986 cites W2109999327 @default.
- W1586150986 cites W2112531650 @default.
- W1586150986 cites W2118262335 @default.
- W1586150986 cites W2159819062 @default.
- W1586150986 cites W2162960825 @default.
- W1586150986 doi "https://doi.org/10.1016/s0021-9258(19)75797-4" @default.
- W1586150986 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/2433278" @default.
- W1586150986 hasPublicationYear "1987" @default.
- W1586150986 type Work @default.
- W1586150986 sameAs 1586150986 @default.
- W1586150986 citedByCount "152" @default.
- W1586150986 countsByYear W15861509862012 @default.
- W1586150986 countsByYear W15861509862013 @default.
- W1586150986 countsByYear W15861509862014 @default.
- W1586150986 countsByYear W15861509862015 @default.
- W1586150986 countsByYear W15861509862016 @default.
- W1586150986 countsByYear W15861509862017 @default.
- W1586150986 countsByYear W15861509862018 @default.
- W1586150986 countsByYear W15861509862019 @default.
- W1586150986 countsByYear W15861509862022 @default.
- W1586150986 countsByYear W15861509862023 @default.
- W1586150986 crossrefType "journal-article" @default.
- W1586150986 hasAuthorship W1586150986A5035727388 @default.
- W1586150986 hasAuthorship W1586150986A5037444081 @default.
- W1586150986 hasBestOaLocation W15861509861 @default.
- W1586150986 hasConcept C181199279 @default.
- W1586150986 hasConcept C185592680 @default.
- W1586150986 hasConcept C2775914622 @default.
- W1586150986 hasConcept C55493867 @default.
- W1586150986 hasConceptScore W1586150986C181199279 @default.
- W1586150986 hasConceptScore W1586150986C185592680 @default.
- W1586150986 hasConceptScore W1586150986C2775914622 @default.
- W1586150986 hasConceptScore W1586150986C55493867 @default.
- W1586150986 hasIssue "3" @default.
- W1586150986 hasLocation W15861509861 @default.
- W1586150986 hasOpenAccess W1586150986 @default.
- W1586150986 hasPrimaryLocation W15861509861 @default.
- W1586150986 hasRelatedWork W1967970523 @default.
- W1586150986 hasRelatedWork W1976336187 @default.
- W1586150986 hasRelatedWork W1987670445 @default.
- W1586150986 hasRelatedWork W1994421171 @default.
- W1586150986 hasRelatedWork W2037909152 @default.
- W1586150986 hasRelatedWork W2116531544 @default.
- W1586150986 hasRelatedWork W2890874837 @default.
- W1586150986 hasRelatedWork W2918716127 @default.
- W1586150986 hasRelatedWork W3022653620 @default.
- W1586150986 hasRelatedWork W4249578969 @default.
- W1586150986 hasVolume "262" @default.
- W1586150986 isParatext "false" @default.
- W1586150986 isRetracted "false" @default.
- W1586150986 magId "1586150986" @default.
- W1586150986 workType "article" @default.