By F. Korte

Nucleic Acids, Proteins and Carbohydrates

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Biol. Chem. 248, 7967 (1973). 84 H, Westphal, R. J. Crouch, Proc. Nat. Acad. Sci. S. 72, 3077 (1975). 77 L. A. Heppel, P. R. Whitfeld, R. Markham, Biochem. J. 85 R. A. Kramer, M. Rosenberg, J. A. Steitz, J. Mol. 50, 8 (1955). Biol. 89, 767 (1974). 78 F. Tamanoi, T. Uckida> F. Egami* T. Oshirna, J. 86 M. Rosenberg, R. A. Kramer, J. A. Steitz, J. Mol. Biochem. 80, 27 (1976). Biol. 3:3 87 88 cell of E. coli in addition to RNase III · . RNase H was first discovered in calf thymus tissue by Hausen and Stein69.

The single-stranded DNA is a much poorer substrate than doublestranded DNA. RNA and synthetic polyribonucleotide inhibit acid DNase as well as some bacterial DNases. The bond specificity in the initial phase is not yet known because of tech­ nical difficulties involved in the determination of the terminal nucleotide in fragments longer than 200 nucleotide units, but those in the middle and terminal phase have been investigated in some laboratories. Vaneko and Laskowski3,21 showed that during the early stage of diges­ tion the linkage d(G-Gp) was most favored by acid DNase and d(G-Cp) was a close second; at the later stage d(A-Cp) and d(A-Gp) bonds were somewhat favored and at the terminal stage the randomness of cleavages increased.

J. Biochem. 43, 405 (1974). 93 K. Moiling, D. P. Bolognesi, H. Bauer, W. Busen, H. W. Plassmann, P. Hausen, Nature New Biol. 234, 240 (1971). 94 /. P. Leis, I. Berkower, J. Hurwitz, Proc. Nat. Acad. Sci. S. 70, 466 (1973); D. P. Grandgenett, M. Green, J. Biol. Chem. 249, 5148 (1974). 95 D. Baltimore, D. F. Smoler, J. Biol. Chem. 247, 7282 (1972). 98 ΛΓ. , Vol. 4, p. 313, Academic Press, New York, London (1971). 97 A. Bernardi, G. , Vol. 4, p. 329, Academic Press, New York, London (1971). Both enzymes have been widely used for nucleic acid research because of the sequential degrada­ tion with distinct polarity of 3'—>5' or 5'—>3'.

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