Biomedical subjects

K Kusui

Publications and source records attributed to K Kusui.

11 recordsLinked to original sources

PubMed1995

Role of terminal galactose residues in N-linked sugar chains of sheep erythrocyte membrane glycoproteins in rosette formation with T lymphocytes.

In this study, we found that rosette formation of T lymphoblastic Molt-3 cells with sheep erythrocytes is inhibited by addition of membrane glycoproteins which were solubilized from sheep erythrocyte ghosts by the lithium diiodosalicylate extraction methods. Their rosetting inhibitory activity was markedly reduced by digestion with N-glycanase, but not with O-glycanase. The inhibitory activity was also reduced by beta-galactosidase digestion, while it was enhanced by desialylation. These observations indicate that nonreducing terminal galactose residues of N-linked sugar chains included in membrane glycoproteins on sheep erythrocytes are important for rosette formation with T lymphocytes.

Animals↗

PubMed1991

Purification and characterization of a carbohydrate-binding peptide from Bauhinia purpurea lectin.

In order to examine the correlation between the amino acid sequence and sugar binding specificity of Bauhinia purpurea lectin (BPA), a galactose and lactose binding lectin, a peptide which interacts with lactose was purified from an Asp-N endoproteinase digest of BPA by means of affinity chromatography on a column of lactose-Sepharose. The amino acid sequence of this peptide is Asp-Thr-Trp-Pro-Asn-Thr-Glu-Trp-Ser. A tryptic fragment having the ability to interact with lactose was also purified and found to contain the above sequence, consisting of 9 amino acids. The chemical synthesis of this peptide was carried out by the solid-phase method and the synthetic peptide was found to exhibit lactose binding activity in the presence of calcium.

Amino Acid Sequence↗

PubMed1991

cDNA cloning and expression of Bauhinia purpurea lectin.

Bauhinia purpurea lectin (BPA) was purified from seeds of B. purpurea alba. The purified lectin was digested with an endoproteinase, Asp-N, or trypsin and then the amino acid sequences of the resultant fragments were analyzed. Furthermore, a cDNA library for BPA was constructed using RNA isolated from germinated Bauhinia purpurea seeds. By gene cloning, the nucleotide sequence of BPA cDNA and its deduced amino acid sequence were analyzed. The cloned BPA cDNA comprised 1,152 nucleotides and the open reading frame of the cDNA encodes a polypeptide of 290 amino acids including a signal peptide composed of 28 amino acids. BPA expressed in Escherichia coli showed a relative molecular mass of 29 kDa on sodium dodecyl sulfate-polyacrylamide gel. On comparison of its sequence with those of other leguminous seed lectins, BPA showed high homology to the others.

Amino Acid Sequence↗

PubMed1975