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Biomedical subjects

N Ui

Publications and source records attributed to N Ui.

At least 37 records · Page 2Linked to original sources
PubMed1977

Bioaffinity chromatography of thyrotropin using immobilized concanavalin A.

The behavior of crude preparations of whale and bovine thyrotropins was studied on an affinity column packed with concanavalin A-Sepharose. Only a small portion of the proteins applied was adsorbed to the column and eluted quantitatively with 0.5 M methyl-alpha-D-glucoside or -mannoside. Immunoreactive as well as hormonally active thyrotropin was recovered exclusively in the absorbed fraction. The usefulness of this chromatographic procedure for the group separation of pituitary glycoprotein hormones is discussed.

Animals↗
PubMed1977

Purification and properties of four biologically active components of whale luteinizing hormone.

Four biologically active components of luteinizing hormone (LH), designated as LH I, II, III, and IV, were isolated from whale pituitary glands. These components migrated as single bands with different mobilities in disc electrophoresis, and their isoeletric points were at pH 8.1, 8.3, 8.5, and 8.7, respectively. Their amino acid and carbohydrate compositions showed close similarity. The molecular weight of whale LH was determined to be 31,000 by sedimentation equilibrium, and no difference was detected among the four components. The molecular properties of whale LH were compared with the previously reported data for LH from other animal species.

Amino Acids↗
PubMed1976

The presence of N-terminal pyroglutamyl residues in hog thyroglobulin.

A method was devised to isolate N-terminal peptide fragments from the polypeptide chains constituting thyroglobulin even in the case when the terminal amino groups are naturally blocked, for instance, acylated. Reduced and carboxymethylated hog thyroglobulin was first acetylated and digested with thermolysin. The blocked N-terminal peptide fragments were separated from the unblocked N-terminal fragments by column chromatography on Dowex 50, then on Dowex 1 after dinitrophenylation, and finally fractionated into ten fractions by paper chromatography after gel filtration on Sephadex G-10. Structural analyses by enzymic or partial acid hydrolysis of these peptide fractions failed to detect N-terminal acetyl amino acid. Instead, pyroglutamyl peptides including pyroglutamylleucine were found. By the same method, acetylated lysine and glycine were identified for chicken lysozyme and horse myoglobin, respectively. The use of thermolysin because of its unique specificity, and the possible relevance of the present result to the previous data on the N-terminal analysis of thyroglobulin are discussed.

Amino Acid Sequence↗
PubMed1976

Purification and properties of whale thyroid-stimulating hormone III. Properties of isolated multiple components.

Properties of the four purified components of whale thyroid-stimulating hormone (TSH) have been compared. The amino acid composition shows close similarity among these components. Their hexosamine and sialic acid contents are of the same magnitude, whereas the neutral sugar composition differs somewhat from each other. The molecular weight of whale TSH determined by sedimentation equilibrium is 29,000, and no difference in molecular weight as well as in Stokes radius as determined by gel filtration has been detected among these four components. The amino acid and carbohydrate compositions of whale TSH resemble those of TSH from other species, especially those of non-primate mammalian TSH. Whale TSH contains, unlike bovine TSH but like human TSH, 1-2 residues of sialic acid as a constituent carbohydrate.

Amino Acids↗