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Cytochemical Quantification of Physiologic Regulation of Oxyntic Cell Carbonic Anhydrase a
dc.contributor.authorVinik, Aaron I.en_US
dc.contributor.authorHeldsinger, A. A.en_US
dc.date.accessioned2010-06-01T19:38:14Z
dc.date.available2010-06-01T19:38:14Z
dc.date.issued1984-06en_US
dc.identifier.citationVINIK, A. I.; HELDSINGER, A. A. (1984). "Cytochemical Quantification of Physiologic Regulation of Oxyntic Cell Carbonic Anhydrase a ." Annals of the New York Academy of Sciences 429(1 Biology and Chemistry of the Carbonic Anhydrases ): 592-596. <http://hdl.handle.net/2027.42/72772>en_US
dc.identifier.issn0077-8923en_US
dc.identifier.issn1749-6632en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/72772
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6430197&dopt=citationen_US
dc.format.extent221998 bytes
dc.format.extent3109 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.publisherBlackwell Publishing Ltden_US
dc.rights1984 New York Academy of Sciencesen_US
dc.titleCytochemical Quantification of Physiologic Regulation of Oxyntic Cell Carbonic Anhydrase aen_US
dc.typeArticleen_US
dc.subject.hlbsecondlevelScience (General)en_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Internal Medicine University of Michigan Medical School Ann Arbor, Michigan 48109en_US
dc.identifier.pmid6430197en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/72772/1/j.1749-6632.1984.tb12393.x.pdf
dc.identifier.doi10.1111/j.1749-6632.1984.tb12393.xen_US
dc.identifier.sourceAnnals of the New York Academy of Sciencesen_US
dc.identifier.citedreferenceMaren, T. 1967. Carbonic anhydrase: Chemistry, physiology and inhibition. Physiol. Rev. 47: 597 – 781.en_US
dc.identifier.citedreferenceCross, S. 1970. Ultrastructural localization of carbonic anhydrase in rat stomach parietal cells. Histochemistry 22: 219 – 225.en_US
dc.identifier.citedreferenceSugai, W. & S. Ito. 1980. Carbonic anhydrase, ultrastructural localization in the mouse gastric mucosa and improvements in the technique. J. Histochem. Cytochem. 28 ( 6 ) 511 – 525.en_US
dc.identifier.citedreferenceLÖnnerholm, G. 1977. Carbonic anhydrase in the intestinal tract of the guinea pig. Acta. Physiol. Scand. 99: 53 – 61.en_US
dc.identifier.citedreferenceLoveridge, N. 1978. A quantitative cytochemical method for measuring carbonic anhydrase. Histochem. J. 10: 361 – 372.en_US
dc.identifier.citedreferenceShapiro, B., K. Pienta, A. Heldsinger & A. I. Vinik. 1981. Somatostatin is an agonist and noncompetitive antagonist of gastrin in oxyntic cell function. Endocrinology 109 ( 4 ): 1117 – 21.en_US
dc.identifier.citedreferenceVinik, A. I., L. J. Klaff B. A. Heldsinger. 1979. A comparison of potency of acid secretagogues in the activation of carbonic anhydrase (CA) in guinea pig parietal cells. Clin. Res. 27: 636A.en_US
dc.identifier.citedreferenceWalker, W., A. I. Vinik, A. A. Heldsinger & R. Kaveh. 1983. The role of calcium and calmodulin in activation of the oxyntic cell by histamine and carbamylcholine in the guinea pig. J. Clin. Invest. 72: 955 – 964.en_US
dc.identifier.citedreferencePuscas, I., A. Chiu, G. H. Buzas, L. Voicu, P. Contrasiv, G. Mihalas, L. Veress, M. Chiss, P. Suranyi, M. Domuta, M. Simonca, O. Arcelean, O. Pascu & M. Rocsin. 1980. Contributions to the elucidation of gastric acid secretory mechanisms, carbonic anhydrase and histamine H 2 receptors. Rev. Roum. Biochem. 17 ( 1 ): 57 – 75.en_US
dc.identifier.citedreferenceSoll, A. H. 1978. The actions of secretagogues on oxygen uptake by isolated mammalian parietal cells. J. Clin. Invest. 61: 370 – 380.en_US
dc.identifier.citedreferenceHersey, S. J. 1974. Interactions between oxidate metabolism and acid secretion in gastric mucosa. Biochem. Biophys. Acta 344: 157 – 203.en_US
dc.identifier.citedreferenceFellenius, E., T. Berglindh, G. Sachs, L. Olbe, B. Elander, S. E. Sjostrand & B. Wallmark. 1981. Substituted benzimidazoles inhibit acid secretion by blocking the H + + K + - ATPase. Nature 290: 159 – 161.en_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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