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Y Hanaoka

Publications and source records attributed to Y Hanaoka.

6 recordsLinked to original sources
PubMed1992

Amphibian lutropin from the bullfrog Rana catesbeiana. Complete amino acid sequence of the beta subunit.

The amino acid sequence of lutropin (LH) beta subunit of an amphibian, the bullfrog Rana catesbeiana, has been determined. The primary structure was determined by sequencing the intact protein (residues 1-44) and peptides originated by cyanogen bromide cleavage and lysyl endopeptidase digestion. 12 cysteine residues are conserved in the bullfrog and mammalian LH beta subunit. One sugar-chain-binding site at Asn-8 is also conserved in the bullfrog and in all mammals except humans. This glycoprotein is composed of 112 amino acid residues with a molecular mass of 12675 Da, considering the six cystine bridges and excepting the sugar chain. The bullfrog beta subunit has approximately 50% sequence identity with that of mammals and with the fish gonadotropin beta subunit, and about 40% with bullfrog follicle-stimulating hormone beta subunit.

Amino Acid Sequence↗
PubMed1992

The complete amino acid sequence of the follitropin beta-subunit of the bullfrog, Rana catesbeiana.

The amino acid sequence of the bullfrog, Rana catesbeiana, follitropin beta-subunit has been determined by sequencing the intact protein (residues 1-39) and peptides originated by lysyl endopeptidase and pepsin. Twelve cysteine residues and two sugar chain binding sites at Asn-5 and Asn-22 are positional identities with bullfrog and mammalian beta-subunits. The bullfrog FSH beta-subunit is composed of 107 amino acid residues with a molecular mass of 11,782 Da, including the six cystine bridges and excepting the sugar chain. The bullfrog FSH beta-subunit has approximately 60% sequence identity with that of mammals and 40% with the fish gonadotropin beta-subunit. Conserved sequences among mammals (residue numbers 33-55 and 66-71) extensively differed from those of the bullfrog.

Amino Acid Sequence↗
PubMed1978

Biochemical and morphological comparison of two tumour-cell-aggregation factors from rat ascites hepatoma cells.

Two tumour-cell-aggregation factors, derived from rat ascites hepatoma cells, had different antigenicity; one was not absorbed by immunoadsorbent chromatography with anti-rat serum antibody and the other was. Their activities were both lost by digestion with trypsin, but remained unchanged by oxidation with periodate, suggesting the role of the protein portions in their molecules. The potency of the unabsorbed factor was inhibited specifically by alpha-methyl-D-mannoside or D-mannose, while that of the absorbed factor was inhibited specifically by N-acetyl-D-glucosamine, suggesting that these carbohydrates may be concerned with the respective receptor structures at the tumour-cell surface. The unabsorbed factor induced not only cell aggregation (as shown in the form of simple apposition) but also cell adhesiveness characterized by development of intermediate junctions, desmosomes and tight junctions, while the absorbed factor produced only simple apposition, suggesting their functional difference.

Animals↗
PubMed1977

Primary action of steroid hormone at the surface of amphibian oocyte in the induction of germinal vesicle breakdown.

An insoluble steroid derivative was prepared by the coupling of desoxycorticosterone with aminoethylated agarose beads. When the naked full-grown Xenopus oocytes were incubated in contact with the steroid-bound agarose beads, the dissociation of oocyte nuclei or the initial step in the maturation of amphibian oocyte was induced in 30-100% of total oocytes. The induction did not occur in the oocytes covered with follicle cells and when the naked oocytes were placed apart from the steroid-bound agarose beads in the medium. The above findings confirmed that the oocyte surface was a primary site for this particular steroid action, eliminating the possibility of participation of free steroid artifactually released from the agarose. The 105,000g supernatant fraction of oocytes showed no sign of the presence of steroid receptor. This was not inconsistent with the assumption mentioned above.

Animals↗
PubMed1976

Characterization of tumour cell aggregation promoting factor from rat ascites hepatoma cells: Separation of two factors with different antigenic property.

The previously described glycoprotein that promotes tumour cell aggregation, derived from rat ascites hepatoma cells and capable of partial purification by chromatography, was found to be a mixture of 2 factors with different antigenic property. One was not absorbed by immunoadsorbent chromatography with anti-rat serum antibody and the other was. The action of the unabsorbed factor was clearly more potent than that of the absorbed factor. Both the factors were found in the serum of tumour bearing rats and the action of the unabsorbed factor was also more potent than that of the absorbed factor; its amount increased with time after i.p. inoculation of the cells. The serum of healthy rats contained the absorbed factor but not the unabsorbed factor. It was thus assumed that the unabsorbed factor was associated with the hepatoma cell surface itself and released into the serum, while the absorbed factor was associated with serum protein coating the cell.

Animals↗