Purification and characterization of testosterone-binding globulin of canine serum.

• SUZUKI Yasuyuki

  Department of Biochemisry, Kinki University School of Medicine

• OKUMURA Yoshiji

  Department of Biochemisry, Kinki University School of Medicine

• SINOHARA Hyogo

  Department of Biochemisry, Kinki University School of Medicine

Abstract

Testosterone-binding globulin (TeBG) of canine serum was purified to apparent homogeneity by affinity chromatography on testosterone-17α-ethynylcarboxyaminoethyl-Sepharose 4 B followed by hydroxyapatite column chromatography. Canine TeBG was a glycoprotein containing 5.5% carbohydrates. Equilibrium sedimentation analysis in the presence and absence of 6M guanidine hydrochloride gave molecular weights of 40, 000 and 76, 000, respectively, suggesting that native TeBG consists of two subunits. Equilibrium dissociation constants at 0°C for testosterone and dihydrotestosterone were estimated to be 5.58×10^-8M and 1.43×10^-8M, respectively, and the number of binding site per native molecule was approximately unity for both androgens. Canine TeBG had virtually no affinity for estradiol, progesterone, or cortisol. Canine TeBG did not cross-react with a rabbit antiserum raised against bovine TeBG.

Journal

• J Biochem (Tokyo)

  J Biochem (Tokyo) 85 (5), 1195-1203, 1979

  The Japanese Biochemical Society

Details

• CRID: 1571980078046283520
• NII Article ID: 130003419202
• ISSN: 0021924X
• Web Site: https://jlc.jst.go.jp/DN/JALC/00339923872?from=CiNii
• Text Lang: en
• Data Source:
  • CiNii Articles