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CHRISTOPHER J. LYNCH, WILLIAM A. BRENNAN, JR., THOMAS C. VARY, NICK CARTER, AND SUSANNA J. DODGSON Department of Cellular and Molecular Physiology, College of Medicine, The Pennsylvania State University, Hershey 17033; Department of Physiology, School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104; and Department of Child Health, St. Georgeâs Hospital Medical School, London SW1 7 ORE, United Kingdom Lynch, Christopher J., William A. Brennan, Jr., Thomas C. Vary, Nick Carter, and Susanna J. Dodgson. Carbonic anhydraseIII in Zucker rats. Am. J. Physiol. 264 (Endocrinol. Metab. 27): E621-E630, 1993.-Proteins from 5 to 7-wk-old and Zucker rats were separatedby onedimensionalsodiumdodecyl sulfate (SDS) and two-dimensional SDS-isoelectric focusing-polyacrylamide gel electrophoresis. Laser densitometry revealed an obesity-related decrease the in concentration of a 28-kDa cytosolic adipocyte protein, the most abundant protein in adipocytes from Zucker rats. Microsequencing revealed the identity of this protein to be carbonic anhydrase III (CA III). The identity and obesity-related decrease was further confirmed using isoform-specific antisera and CA III enzyme activity measurements made by 180 mass spectrometry. Immunoblotting studiesalsorevealedthat CA III is presentin at leasttwo chargeisoformsin adipocytes.Our data indicate that Zucker rat adipocytesmay representthe richest source of CA III in nature (24% of the cytosolic protein content). An
AJP - Endocrinology and Metabolism – The American Physiological Society
Published: Apr 1, 1993
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