Studies of the limited degradation of mucus glycoproteins. The effect of dilute hydrogen peroxide

• Published in: Biochemical journal Vol. 211; no. 2; pp. 323 - 332
• Main Authors: Creeth, J M, Cooper, B, Donald, A S, Clamp, J R
• Format: Journal Article
• Language: English
• Published: England 01.05.1983
• Subjects: Amino Acids - analysis; Blood Group Antigens; Carbohydrates - analysis; Centrifugation, Density Gradient; Chemical Phenomena; Chemistry; cyst; Edetic Acid - pharmacology; Electrophoresis, Polyacrylamide Gel; Female; glycoproteins; Glycoproteins - metabolism; histidine; hydrogen peroxide; Hydrogen Peroxide - pharmacology; Mucus - metabolism; Muramidase - metabolism; Myosins - metabolism; Ovarian Cysts - metabolism; ovary; Oxidation-Reduction
• ISSN: 0264-6021; 1470-8728
• DOI: 10.1042/bj2110323

1. The action of dilute H2O2 on a series of ovarian-cyst glycoproteins and glycopolypeptides was investigated. 2. Both native glycoproteins and the glycopolypeptides were carbohydrate-rich, of relatively low molecular weight and of simple structure. 3. At pH 5.6 and 37 degrees C, exposure to H2O2 for a limited time brought about a partial degradation, the molecular weight being decreased by 2-4-fold. 4. Carbohydrate analysis showed very little change in the oligosaccharide moiety, apart from a small decrease in sialic acid in some samples. 5. Amino acid analysis showed minor changes in serine, threonine and proline contents, but almost total loss of histidine. Concomitantly, there was a small gain in aspartic acid. 6. Myosin, examined at both pH 5.7 and 6.7, exhibited generally similar behaviour, there being losses of other amino acid residues as well as histidine: the viscosity was decreased to a low value, and a range of peptides of widely varying size was produced. 7. It is suggested that attack on the histidine residue, with partial conversion into aspartic acid, is accompanied by scission of the histidyl peptide bond.