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| Content Provider | PubMed Central |
|---|---|
| Author | Boursnell, J. C. Hartree, E. F. Briggs, P. A. |
| Abstract | 1. Moving-boundary electrophoresis of the mucin from the Cowper's gland of the boar revealed a sharp single peak at pH values from 1.1 to 9.0 and an isoelectric point of 1.1. 2. Neuraminidase treatment of the mucin, which removed at least 96% of the sialic acid groups, decreased the electrophoretic mobility at pH4 from −7.4×10−5 (for the mucin) to −0.64×10−5cm2V−1s−1. 3. Ultracentrifugal sedimentation values of s 20,w showed a marked dependence on concentration. A hyperfine peak, similar to that given by ovine submaxillary secretion, persisted throughout the run at higher concentrations. Ultracentrifugal studies further showed a very low value for the diffusion coefficient (D 20,w −1.57×10−8cm2/s). 4. Calculation of the approximate molecular weight from comparable s 20,w and D 20,w values gave a provisional value of 6.5×106. 5. Two proteins present in the boar vesicular secretion known as protein A and protein H (the haemagglutinating protein) were shown to promote the swelling of the mucin to form the characteristic rigid elastic gel of boar semen. It is suggested that protein A molecules particularly (mol.wt. 2.8×104) cross-link with the long molecules of the mucin to form the seminal gel. |
| Starting Page | 981 |
| File Format | |
| ISSN | 14708728 |
| e-ISSN | 14708728 |
| Journal | Biochemical Journal |
| Issue Number | 5 |
| Volume Number | 117 |
| Language | English |
| Publisher Date | 1970-05-01 |
| Access Restriction | Open |
| Subject Keyword | Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Molecular Biology Biochemistry |
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