By F. F. (Editor); Nord
Advances in Enzymology and comparable components of Molecular Biology is a seminal sequence within the box of biochemistry, delivering researchers entry to authoritative studies of the most recent discoveries in all parts of enzymology and molecular biology. those landmark volumes date again to 1941, supplying an unmatched view of the ancient improvement of enzymology. The sequence bargains researchers the most recent knowing of enzymes, their mechanisms, reactions and evolution, roles in complicated organic approach, and their software in either the laboratory and undefined. each one quantity within the sequence gains contributions by way of best pioneers and investigators within the box from all over the world. All articles are conscientiously edited to make sure thoroughness, caliber, and clarity.
With its wide selection of themes and lengthy old pedigree, Advances in Enzymology and comparable components of Molecular Biology can be utilized not just through scholars and researchers in molecular biology, biochemistry, and enzymology, but in addition by means of any scientist drawn to the invention of an enzyme, its houses, and its purposes.
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Additional info for Advances in Enzymology and Related Areas of Molecular Biology, Volume 31
It is known that acid DNase is very rich in amide groups (121) and that deaniidation can occur a t low pH in a number of proteins. To test this hypothesis, three acid deoxyribonuclease preparations were made using modifications of the procedure described above. 15M NaCl. 05M H2S04 in the tissuehomogenization step. All these preparations were carried through the chromatographic purification (procedure C) and the amount of A and B components were estimated from the elution curve obtained in the CM-Sephadex chromatography.
3; upon acid hydrolysis and two-dimensional paper chromatography, the amino acid pattern was qualitatively identical to similar chromatograms prepared with bovine albumen. 6% of hexose was found to be present. 5 3 6 6 6 6 6 58 P. U. ANOELETTI, R. LEVI-MONTALCINI, P. CALISSANO additional lines of evidence support the view that the biological activity is associated with a protein: (1) the biological activity was completely destroyed upon incubation with proteolytic enzymes (trypsin, pepsin, chymotrypsin) ; (2) the biological activity was lost upon incubation with antiserum to snake venom.
T h b e de 3bme Cycle, Universite de Strasbourg, 1965. 77. , Can. J . Bwchem. (in press). 78. , J . Mol. , 11, 141 (1965). 79. , Biochem. Biophys. Res. , go, 555 (1965). , Bull. Soe. Chim. , 60, 366 (1968). 80. ,and Sadron, C.. Biochim. Bwphys. Acta, 49, 1 (1961). 81. , Nature, 188, 228 (1960). 82. , Nature, 191, 809 (1961). 83. Wilkins, M. H. , Science, 401,3570 (1963). 84. , A . Baselli Conference on Nucleic Acids and their Role i n Biology, Milan (September 1963), 1964, p. 62. 85. ,Biochemistry, S, 1411 (1964).