Affinity liquid chromatography and capillary electrophoresis of seminal plasma proteins

✍ Scribed by Tereza Vařilová; Hana Seménková; Pavel Horák; Milan Maděra; Vera Pacáková; Marie Tichá; Karel Štulík

• Publisher: John Wiley and Sons
• Year: 2006
• Tongue: English
• Weight: 687 KB
• Volume: 29
• Category: Article
• ISSN: 1615-9306
• DOI: 10.1002/jssc.200500405

✦ Synopsis

Abstract

Interactions of boar, bull, and human seminal plasma proteins with heparin and phosphorylcholine were studied by affinity LC using heparin immobilized to a Toyopearl support. A step gradient elution from 0.15 to 1.50 M NaCl was employed to elute the seminal plasma proteins. Relative amounts of the heparin‐binding fraction of seminal plasma proteins (H+) in seminal plasma of three species were determined. Further on, the fraction of seminal plasma proteins interacting with phosphorylcholine‐binding proteins (P+) was evaluated. P+ proteins were not found in human seminal plasma and their highest amount was present in bull seminal plasma. A CE method was developed for separation of seminal plasma proteins. Various capillaries and separation conditions were tested; the best resolution was obtained in a bare‐silica capillary, with a micellar system consisting of a 0.02 M borate buffer and 0.05 M SDS pH 10.0. The optimized conditions were applied to the identification of the components in boar plasma.