The macromolecular structure of human cervical-mucus glycoproteins. Studies on fragments obtained after reduction of disulphide bridges and after subsequent trypsin digestion - PubMed (original) (raw)

The macromolecular structure of human cervical-mucus glycoproteins. Studies on fragments obtained after reduction of disulphide bridges and after subsequent trypsin digestion

I Carlstedt et al. Biochem J. 1983.

Abstract

Human cervical-mucus glycoproteins (mucins) were extracted with 6 M-guanidinium chloride in the presence of proteinase inhibitors and purified by isopycnic density-gradient centrifugation. The whole mucins (Mr approx. 10 X 10(6] were degraded into 'subunits' (Mr approx. 2 X 10(6] by reduction of disulphide bonds. Trypsin digestion of the 'subunits' produced glycopeptides with Mr approx. 380000, which appear to be rod-like with a length of approx. 105 nm. The relationship between the radius of gyration and the Mr value obtained by light-scattering for whole mucins, 'subunits' and 'domains' suggest that cervical-mucus glycoproteins are linear flexible macromolecules composed of, on the average, four or five 'domains'/subunit and four subunits/whole mucin macromolecule. The shape-dependent particle scattering function for the whole mucins and the 'subunits' are in accordance with that of a linear flexible chain. No evidence for a branched or a star-like structure was found. A tentative model for cervical mucins is proposed.

PubMed Disclaimer

Similar articles

Cited by

References

    1. Biochem J. 1970 Jan;116(1):27-34 - PubMed
    1. J Biol Chem. 1971 Jan 25;246(2):430-5 - PubMed
    1. Fertil Steril. 1977 Jan;28(1):53-8 - PubMed
    1. Biochemistry. 1977 Apr 5;16(7):1518-24 - PubMed
    1. Biochem J. 1977 Dec 1;167(3):557-69 - PubMed

Publication types

MeSH terms

Substances

LinkOut - more resources