Titlebook: Metabolism and Enzymology of Nucleic Acids; Including Gene Manip Ján Zelinka,Jozef Balan Book 1988 Plenum Press, New York 1988 Chloroplast.

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Nucleoside Phosphotransferase and Nuclease S1 Two Enzymes with Acylphosphate Intermediates, But DifThis is a report on two enzymes hydrolyzing the phosphomonoester bond of nucleotides via acylphosphate intermediates [1, 2]: nucleoside phosphotransferase with retention [3] and nuclease S. with inversion of absolute configuration [4].

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A Site-Mutated , Gene Expression Construct: Impairment of Ribosomal Function,Ribosomal RNA serves as the backbone in ribosomal assembly and also, at least to some degree, as an active component of the mature ribosome. The introduction of nucleotide changes (e. g., by site-directed mutations) clearly offers the most promising tool for elucidating the function of ribosomal RNA.

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Expression of Prochymosin cDNA in ,,Calf chymosin is an aspartyl protease whose specific activity in inducing the coagulation of milk plays an important role in cheese manufacture. Cloning and expression of calf prochymosin in . coli has been reported from several laboratories (e. g. Nishimori .., 1982, Emtage .., 1983, Liebscher .., 1985, Sedlác?ek .., 1987).

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The X-Ray Analysis of Ribonuclease Sa,n determined by X-ray analysis. The electron density that was finally interpreted was calculated with phases obtained by multiple isomorphous replacement technique and solvent flattening at a resolution of 2.5 A. Refinement against 1.8 A data yields R factor of 0.172 and 0.184 for the native and com

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Cloning, Expression and Nucleotide Sequence of a Gene Encoding a Second Thioredoxin from ,,of the thioredoxins is the presence of a disulfide bridge at the active site forming a fourteen-membered ring with the sequence -cys-gly-pro-cys-. The complete primary structures of thioredoxins from several sources have been determined and they exhibit a high degree of homology (Holmgren, 1968; Men