Tamm-Horsfall urinary glycoprotein. The subunit structure

Biochem J. 1970 Nov;120(2):425-32. doi: 10.1042/bj1200425.

Abstract

1. Subunit molecular weights of 76000-82000 were obtained for native and alkylated Tamm-Horsfall glycoprotein by gel filtration on Sephadex G-200 in the presence of sodium dodecyl sulphate. 2. A further estimate of the subunit molecular weight of 79000+/-4000 was obtained by disc gel electrophoresis in sodium dodecyl sulphate. 3. A minimum value of the chemical molecular weight of 79000+/-6000 was obtained from the number of N-terminal amino acids released by cyanogen bromide cleavage of the glycoprotein. 4. Similar values were obtained for the subunit molecular weight of Tamm-Horsfall glycoprotein from patients with cystic fibrosis. 5. On ultracentrifugation both in 1.0% sodium dodecyl sulphate and in 70% formic acid, Tamm-Horsfall glycoprotein sedimented as a single component, slightly faster than serum albumin. 6. On reduction of the disulphide bonds the same subunit molecular weight was obtained, which suggested that these bonds are intrachain.

MeSH terms

  • Adult
  • Amino Acids / analysis
  • Chromatography, Gel
  • Cyanides
  • Cystic Fibrosis / urine
  • Detergents
  • Dextrans
  • Electrophoresis, Disc
  • Formates
  • Glycoproteins / analysis
  • Glycoproteins / urine*
  • Humans
  • Male
  • Molecular Weight
  • Oxidation-Reduction
  • Serum Albumin
  • Sulfides
  • Ultracentrifugation

Substances

  • Amino Acids
  • Cyanides
  • Detergents
  • Dextrans
  • Formates
  • Glycoproteins
  • Serum Albumin
  • Sulfides