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Biomedical subjects

G Hocman

Publications and source records attributed to G Hocman.

At least 37 records · Page 2Linked to original sources
PubMed1978

Heart proteins. Prevention of the denaturation of actomyosin by sodium glutamate.

The storage of actomyosin isolated from bovine heart for one week either at +4 degrees or frozen at -5 degrees results in deep structural changes in the molecule of actomyosin, while storage of the actomyosin at the mentioned temperatures in the presence of sodium glutamate preserved the characteristic structure of actomyosin molecule as revealed by electron microscopy.

Actomyosin↗
PubMed1977

Apparent electric charge of protein molecules. Human thyroxine - binding proteins.

1. By comparison of electrophoretic mobilities of two different charged particles under the same conditions the net elementary electrostatic charge of one particle could be calculated when the charge of the other is known. 2. The electrophoretic mobility of human thyroxine - binding globulin does not depend upon the concentration of Tris - HCl buffer in the range 0.05 to 0.20 molar. The value of this mobility is 0.078 and 0.083 cm2 vol(-1) hour(-1) at pH 7.0 and 8.6, respectively. 3. The net elementary electrostatic charge of the human thyroxine - binding globulin appears to be approximately 22 negative elementary electrostatic units in mild alkaline solutions.

Electrochemistry↗
PubMed1977

Protein determination: a comparison of several methods.

A comparison of four methods for the determination of total proteins is presented from the following points of view: - sensitivity; - specificity; - amount of work, chemicals, time and equipment needed for the performance of the determination. The following tests have been examined; Tombs' (absorbancy at 210 nm); Waddell's (difference in absorbancy between 215 and 225 nm); Warburg's (absorbancy at 280 nm); Lowry's (absorbancy at 500 nm after the reaction with phenol reagent). The authors recommend Tombs' method for its outstanding sensitivity, specificity and simplicity as the best of the four.

Animals↗