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Nucleotide sequence of the tail tube structural gene of bacteriophage T4.
The nucleotide sequence of gene 19 of bacteriophage T4, the structural gene of the tail tube protein, was determined by both the dideoxy and the Maxam-Gilbert methods, and the implication was examined by an S1 nuclease protection experiment. Expand
Primary structure of Streptomyces griseus metalloendopeptidase II.
Based on the sequence comparison of SGMPII and other bacterial metalloproteases, the structural basis for the differences in substrate specificity and stability between SGMP II and other thermolysin-like proteases is discussed. Expand
Structural and functional study of an Anemonia elastase inhibitor, a "nonclassical" Kazal-type inhibitor from Anemonia sulcata.
The CSH motif-containing derivative of AEI (AEI analogue) was chemically synthesized and exhibited unexpected strong inhibition toward Streptomyces griseus protease B (SGPB), while the AEI analogue scarcely inhibited porcine pancreatic elastase (PPE), even though it exhibited almost the same potent inhibitory activity toward SGPB. Expand
Interactions of Streptomyces serine-protease inhibitors with Streptomyces griseus metalloendopeptidase II.
SGMPII and subtilisin BPN' proved, therefore, to interact with SSI in a competitive manner, despite the difference in the chemical nature of their active sites. Expand
Application of bimane-peptide substrates to spectrofluorometric assays of metalloendopeptidases.
Kinetic parameters of the enzymatic hydrolyses of five kinds of analogous bimane substrates were compared to examine how the nature of neighboring amino acid residues on either side of the cleavable bond affects the catalytic efficiency of each of the metalloendopeptidases. Expand
Affinity chromatography on immobilized anhydrotrypsin: general utility for selective isolation of C-terminal peptides from protease digests of proteins.
The general utility of affinity chromatography for C-terminal peptide isolation is suggested, which is extremely helpful for studies to confirm amino acid sequences deduced from nucleotide sequences of the cDNA (or genomic DNA) of proteins. Expand
Immobilized anhydrochymotrypsin as a biospecific affinity adsorbent for the peptides produced by chymotryptic hydrolysis.
Anhydrochymotrypsin immobilized on Sepharose specifically adsorbed various peptides containing L-tryptophan, L-tyrosine, or L-phenylalanine residues at their carboxy-termini. These peptidesExpand
A novel method for selective isolation of C‐terminal peptides from tryptic digests of proteins by immobilized anhydrotrypsin: Application to structural analyses of the tail sheath and tube proteins
Using this method, the C‐terminal peptides from tryptic digests of the sheath protein and the tube protein of bacteriophage T4 are isolated and the complete primary structures of the two proteins are established. Expand
Affinity chromatography of trypsin and related enzymes. II. An affinity adsorbent containing glycylglycyl-L-arginine.
It was found that alpha- and beta-trypsin could be distinguished and in the presence of arginine and N-substitute arginines, the elution of trypsin was accelerated and the affinities of these compouunds could be compared. Expand