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PubMed · 487598

Derivative electrophoretograms and their applications.

K Okamura
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Abstract

A differentiator was constructed to produce the first and second derivative curves of routine cellulose acetate membrane electrophoretograms of human serum protein. The derivative curves could reveal the presence of multicomponent in each globulin fraction. The "M" components could be detected easily and semiquantitatively, when the cellulose acetate membrane electrophoretic pattern was evaluated by the derivative curves. Utilization of the derivative curves could be a useful adjunct to the detection of an "M" component since the presence of a narrow band produces a sharper peak on the second derivative curve and more indentation on the first derivative curve.

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Blood Protein ElectrophoresisComputersElectrophoresis, Cellulose AcetateHumansJournal Article

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K Okamura. 1979-09-03. Derivative electrophoretograms and their applications.. https://doi.org/10.1016/0009-8981(79)90440-6

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PubMed1979

Protein phosphorlyation in human peripheral blood lymphocytes. Phosphorylation of endogenous plasma membrane and cytoplasmic proteins.

Phosphorylation of endogenous proteins in subcellular fractions of human peripheral-blood lymphocytes was studied by one- and two-dimensional polyacrylamide-gel electrophoresis. Studies using extensively purified subcellular fractions indicated that the endogenous phosphorylating activity in the particulate fractions was derived primarily from the plasma membrane. Electrophoresis of (32)P-labelled subcellular fractions in two dimensions [O'Farrell (1975) J. Biol. Chem.250, 4007-4021] provided much greater resolution of the endogenous phosphoproteins than electrophoresis in one dimension, facilitating their excision from gels for quantification of (32)P content. More than 100 cytoplasmic and 20 plasma-membrane phosphorylated species were observed. Phosphorylation of more than 10 cytoplasmic proteins was absolutely dependent on cyclic AMP. In the plasma membrane, cyclic AMP-dependent phosphoproteins were observed with mol.wts. of 42000, 42000, 80000 and 90000 and pI values of 6.1, 6.3, 6.25 and 6.5 respectively. Phosphorylation of endogenous cytoplasmic and plasma-membrane proteins was rapid with t((1/2))=5-12s at 25 degrees C. Between 40 and 70% of the (32)P was recovered as phosphoserine and phosphothreonine when acid hydrolysates of isolated plasma-membrane phosphoproteins were analysed by high-voltage paper electrophoresis. The presence of cyclic AMP-dependent protein kinase and endogenous phosphate-acceptor proteins in the plasma membranes of lymphocytes provides a mechanism by which these cells might respond to plasma-membrane pools of cyclic AMP generated in response to stimulation by mitogens or physiological modulators of lymphocyte function.

Blood Protein Electrophoresis↗