By F. F. (Editor); Nord

Advances in Enzymology and similar parts of Molecular Biology is a seminal sequence within the box of biochemistry, delivering researchers entry to authoritative reports of the most recent discoveries in all components of enzymology and molecular biology. those landmark volumes date again to 1941, supplying an unequalled view of the historic improvement of enzymology. The sequence deals researchers the most recent realizing of enzymes, their mechanisms, reactions and evolution, roles in complicated organic method, and their software in either the laboratory and undefined. each one quantity within the sequence beneficial properties contributions through major 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 variety of subject matters and lengthy ancient pedigree, Advances in Enzymology and similar parts of Molecular Biology can be utilized not just via scholars and researchers in molecular biology, biochemistry, and enzymology, but in addition by way of any scientist drawn to the invention of an enzyme, its houses, and its purposes.

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108. , Biochim. Biophya. Actu, 81, 547 (1962). 109. , J. ,838, 1135 (1961). 110. , Biochim. Biophya. Acta, 48, 211 (1961). 111. , Collection Czech. Chem. , 88, 2739 (1961). 112. , Collection Czech. Chem. , 87, 1476 (1962). 113. , Comm. 3rd FEBS Meeting, C 66, Academic Press, New York, 1966. 114. ti8tryJ7, 1121 (1968). 115. , in preparation 116. , Nature, 198, 186 (1963). 117. , Biochemistsy, 3, 1419 (1964). 118. , Biochim. Biophya. Acta, 189, 1 (1966). 119. , in Procedures in Nucleic Acid Research, G .

Chemical evidence for the dimeric structure of acid DNase came from an investigation of the tryptic hydrolysate of the enzyme. This was reduced, carboxymethylated, and digested with crystalline trypsin treated with L-1-tosylamido-2-phenethyl-chloromethyl-ketone to inactivate contaminating chymotrypsin (an indispensable precaution in view of the abundance of aromatic amino acid residues in the enzyme). In the map of the digest, 17-19 peptides were found (Fig. 22) as opposed to 32-34 arginine lysine residues found by Bernardi, Appella, and Zit0 (121)in the enzyme of molecular weight 38,000.

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