Biomedical subjects

S Panyim

Publications and source records attributed to S Panyim.

74 records · Page 5Linked to original sources

PubMedDate not supplied

The apparent inhibitor of the protein kinase in the human seminal plasma: an explanation.

The protein kinase in the human seminal plasma, as assayed by its ability to catalyze the transfer of phosphate from [gama-32P]ATP to the protamine, was found to linearly increase with dilution of the seminal plasma. Extrapolation of the enzyme activity to the undiluted seminal plasma indicated that te protein kinase existed in the ejaculate as the inactive enzyme. An inhibitor of the protein kinase was postulated and the results suggested that the inhibitor was a heat-labile macromolecule. However, the linear increase of the protein kinase activity could also be obtained by increasing ATP concentration. In addition, a high Mg+2-dependent ATPase activity was found in the seminal plasma, its activity exhibited inverse relationship with the activity of the protein kinase. The results suggested that the apparent inhibitor of the protein kinase in the human seminal plasma was the destruction of ATP by the ATPase.

Adenosine Triphosphatases↗

PubMedDate not supplied

In vitro specific phosphorylation of the human seminal proteins.

A condition for active phosphorylation of the human seminal proteins was achieved by addition of 0% triton X-100 which inhibited the active ATPase. Analysis of the phosphorylated products by SDS-PAGE revealed that the products at 3 min after ejaculation were consisted mainly of the 72K, 70K, and 50K which changed to 25K, 18K and 17.5K at 30 min. There was massive degradation of the seminal plasma proteins during the first 30 min after the ejaculation, resulting in a generation of smaller molecular weight proteins. Comparison of the protein staining pattern and the autoradiographic pattern suggested that the phosphorylation was protein specific and preferentially occurred on larger molecular weight proteins which were subsequently broken down to those of smaller molecular weight. The protein specific phosphorylation was further demonstrated by the result from a two dimensional gel electrophoresis. The specific phosphorylation suggests that side-chain modification of the seminal proteins may regulate a physiological function of the semen.

Adult↗