Biomedical subjects

J Hirabayashi

Publications and source records attributed to J Hirabayashi.

57 records · Page 4Linked to original sources

PubMed1984

Human placenta beta-galactoside-binding lectin. Purification and some properties.

A beta-galactoside-binding lectin was extracted from human placenta homogenate with lactose solution and purified to apparent homogeneity by affinity chromatography on asialofetuin-Sepharose. The apparent subunit molecular weight of the lectin was 13,800 and its isoelectric point was about 5. Several saccharides containing D-galactose inhibited the hemagglutinating activity. The lectin resembles other vertebrate beta-galactoside-binding lectins in various biochemical characteristics.

Amino Acids↗

PubMed1983

The primary structure of ribonuclease F1 from Fusarium moniliforme.

The primary structure of ribonuclease F1, the guanine specific ribonuclease from Fusarium moniliforme, has been determined. Ribonuclease F1 consists of 106 amino acid residues and has a molecular weight of 10,980. It has a pyroglutamyl residue at the N-terminus. Comparison of the primary structures of four fungal ribonucleases so far sequenced shows that the amino acid sequences around the assumed active site residues are indeed well conserved. However, structurally important half cystine residues are arranged variously.

Amino Acid Sequence↗

PubMedDate not supplied

Specific isolation by anhydrotrypsin-agarose chromatography of a recombinant protein tagged with an affinity tail arginine at the C-terminus.

A characteristic property of anhydrotrypsin, i.e., its ability to strongly bind C-terminal arginine, proved to be useful as a tool for specific enrichment of a recombinant protein. An arginine tail was introduced at the C-terminus, for example, of a human beta-galactoside-binding lectin by site-directed mutagenesis. The resulting mutant recombinant lectin, which retained sugar-binding activity as high as the wild-type lectin, became recognizable by anhydrotrypsin. It was adsorbed on an anhydrotrypsin-agarose column and eluted with benzoylglycylarginine. The added arginine tail could be specifically removed by carboxypeptidase B. When E. coli lyzate containing the mutant lectin was applied to the column more than 10-fold enrichment of the mutant lectin was attained. This procedure should be generally applicable and may be advantageous because the addition of a single arginine residue may have minimal effect on the structure and function of the target protein.

Arginine↗