Modification of an arginine residue of a base-nonspecific ribonuclease from Aspergillus saitoi. 1979

H Watanabe, and K Ohgi, and M Irie

1. A base-nonspecific ribonuclease from Aspergillus saitoi [RNase Ms, EC 3.1.4.23; molecular weight, 12,500] was modified with phenylglyoxal (PG) and 1,2-cyclohexanedione (CHD) in order to determine whether a single arginine residue was involved in the active site of the enzyme. 2. RNase Ms was inactivated by both PG and CHD with concomitant loss of one arginine residue. A competitive inhibitor of RNase Ms, 2',(3')-AMP, protected the enzyme from inactivation by PG. These findings strongly suggest that one arginine residue is involved in the active site of RNase Ms. 3. Difference CD spectra were measured at pH 5.5 for the binding of 2'-AMP and adenosine to native RNase Ms and the CHD- and PG-modified enzyme derivatives to determine the association constants. The arginine modification brought about a marked decrease in the binding affinity of 2'-AMP for the enzyme, but only a slight decrease for adenosine, suggesting that the arginine residue had interacted with the phosphate groups of the substrate.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D002942 Circular Dichroism A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Circular Dichroism, Vibrational,Dichroism, Circular,Vibrational Circular Dichroism
D003512 Cyclohexanones Cyclohexane ring substituted by one or more ketones in any position.
D006037 Glyoxal A 2-carbon aldehyde with carbonyl groups on both carbons. Ethanedial,Ethanedione
D001120 Arginine An essential amino acid that is physiologically active in the L-form. Arginine Hydrochloride,Arginine, L-Isomer,DL-Arginine Acetate, Monohydrate,L-Arginine,Arginine, L Isomer,DL Arginine Acetate, Monohydrate,Hydrochloride, Arginine,L Arginine,L-Isomer Arginine,Monohydrate DL-Arginine Acetate
D001230 Aspergillus A genus of mitosporic fungi containing about 100 species and eleven different teleomorphs in the family Trichocomaceae.
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining

Related Publications

H Watanabe, and K Ohgi, and M Irie
November 1980, Journal of biochemistry,
H Watanabe, and K Ohgi, and M Irie
October 1969, Journal of biochemistry,
H Watanabe, and K Ohgi, and M Irie
July 1979, Journal of biochemistry,
H Watanabe, and K Ohgi, and M Irie
November 1968, Journal of biochemistry,
H Watanabe, and K Ohgi, and M Irie
November 1967, Journal of biochemistry,
H Watanabe, and K Ohgi, and M Irie
June 1969, Journal of biochemistry,
H Watanabe, and K Ohgi, and M Irie
May 1975, Journal of biochemistry,
H Watanabe, and K Ohgi, and M Irie
December 1977, Journal of biochemistry,
H Watanabe, and K Ohgi, and M Irie
April 1973, Journal of biochemistry,
H Watanabe, and K Ohgi, and M Irie
May 1971, Journal of biochemistry,
Copied contents to your clipboard!