PubMed Health⌕ Search

Biomedical subjects

D Yamashiro

Publications and source records attributed to D Yamashiro.

At least 37 records · Page 2Linked to original sources
PubMed1987

Gonadotropin-releasing peptide from human follicular fluid: isolation, characterization, and chemical synthesis.

A gonadotropin-releasing peptide has been isolated from human follicular fluid. Its amino acid composition and sequence are completely different from the hypothalamic lutropin-releasing hormone. It is designated human follicular gonadotropin-releasing peptide and abbreviated as hF-GRP. The primary structure of this peptide (H-Thr-Asp-Thr-Ser-His-His-Asp-Gln-Asp-His-Pro-Thr-Phe-Asn-OH) has been confirmed by chemical synthesis. In the mouse pituitary incubation assay, the ED50 value for follitropin or lutropin release is estimated to be 1.2-1.6 nM.

Body Fluids↗
PubMed1986

Chemical synthesis of alpha-inhibin-92 by the thiocarboxyl segment coupling method.

The amino acid residue peptide, alpha-inhibin-92 (alpha-IB-92), has been synthesized by the thiocarboxyl segment strategy. Three segments were synthesized by the solid phase method, purified, and characterized: [GlyS34]-alpha-IB-92-(1-34) (I), CF3CO-[GlyS65]-alpha-IB-92-(35-65) (II), and Msc-alpha-IB-92-(66-92) (III). All were reacted with citraconic anhydride followed by removal of the Msc group in III to give Ia, IIa, and IIIa, respectively. Peptide IIIa was coupled to IIa by the silver nitrate/N-hydroxysuccinimide procedure and, after removal of uncoupled segments and the trifluoroacetyl group, Ia was coupled followed again by removal of uncoupled segments. Final deblocking to remove citraconyl groups was accomplished under exceptionally mild conditions in aqueous acetic acid. The synthetic product was identical to natural alpha-IB-92 in amino acid analysis, HPLC, gel electrophoresis, and tryptic mapping. The synthetic peptide was indistinguishable from natural alpha-IB-92 in a radioimmunoassay and in an in vitro mouse pituitary assay for measuring suppression of FSH release in the presence of LHRH.

Amino Acid Sequence↗
PubMed1985

Synthetic insulin-like growth factor II.

Human insulin-like growth factor II with 67 amino acid residues and three disulfide bridges has been synthesized by the solid-phase method. Homogeneity of the synthetic product is ascertained by chromatofocusing, high performance liquid chromatography and amino acid analysis. In both radioimmunoassay and radioreceptor assay, the synthetic product is indistinguishable from the natural hormone.

Amino Acids↗
PubMed1985

Radioimmunoassay for an inhibin-like peptide from human seminal plasma.

Antisera raised in rabbits to a synthetic peptide consisting of 31 amino acids with a sequence identical to inhibin-like peptide (ILP) isolated from human seminal plasma afford a highly specific and sensitive radioimmunoassay. Synthetic ILP completely displaces antiserum binding of radioiodinated [Tyr4]-ILP, with half maximal displacement at 36 fmoles ILP/tube. ILP, [Tyr4]-ILP and ILP-(9-31) had essentially equal potency, while ILP-(1-25), ILP-(1-23) and ILP-(1-16) had reduced potency. No cross reactivity was found among a variety of peptide hormones and proteins. Human seminal plasma displaces 50% of [125I-Tyr4]-ILP at dilutions equivalent to 50-250 pl/tube, corresponding to immunoreactive ILP concentration of 0.5-2.5 mg/ml.

Amino Acid Sequence↗
PubMed1985

Chemical synthesis of insulin-like growth factor II.

Human insulin-like growth factor II (IGF-II) with 67 amino acids and three disulfide bridges has been synthesized by the solid-phase method. The synthetic hormone is shown to be homogeneous in high performance liquid chromatography (HPLC), high performance partition chromatography (HPPC), and chromatofocusing. It is indistinguishable from natural hormone in HPLC, peptide map of thermolysin digests, amino acid composition and radioreceptor binding assay. Thus, synthetic and natural IGF-II are identical.

Amino Acid Sequence↗
PubMed1984

Synthesis and biological activity of human inhibin-like peptide-(1-31).

A peptide containing 31 amino acids with inhibin-like activity has been synthesized by the solid-phase method. The synthetic product was shown to be homogeneous in high-performance liquid chromatography and paper electrophoresis. In the mouse pituitary incubation system, the follitropin-suppressing activity of the synthetic peptide was comparable to that of the natural product. It was also active in suppressing lutropin-releasing hormone-induced follitropin release in vivo in immature male rats.

Animals↗
PubMed1984

Synthesis of shrimp red pigment-concentrating hormone analogs and their biological activity in locusts.

Two analogs of the red pigment-concentrating hormone (RPCH) have been synthesized by the solid-phase method: [Thr6]-RPCH (I) and [Tyr4, Thr6]-RCPH (II). Analog I has the same amino acid composition as the second adipokinetic hormone (AKH-II) isolated from locust corpora cardiaca. Bioassay for lipid-mobilizing activity in adult male locusts gave the following increases in hemolymph lipid content: AKH-I, 3.5; I, 2.4; II, 2.9. The biological response shown by I lends support to the conclusion that its sequence is that of the presumptive AKH-II. Replacement of Phe in position 4 by Tyr does not reduce the adipokinetic response.

Animals↗
PubMed1984

Adrenocorticotropin. 57. Synthesis and biological activity of ostrich and turkey hormones.

Synthesis of ostrich and turkey corticotropin (ACTH) has been accomplished by the solid-phase method. Each was identical to the natural hormone in high performance liquid chromatography. Relative potencies in a lipolytic assay in isolated rabbit fat cells were: human ACTH, 100; ostrich ACTH, 53; turkey ACTH, 28. In isolated rat fat cells relative lipolytic potencies were: human ACTH, 100; ostrich ACTH, 2; turkey ACTH, 13. It was concluded that lipolytic potency is sensitive to alterations in structure throughout the entire length of the ACTH sequence in the rat fat cell assay.

Adipose Tissue↗
PubMed1984

Human beta-endorphin. Synthesis and biological activity of analogs with modifications in residue positions 3, 4 or 5.

Three analogs of human beta-endorphin (beta h-EP) have been synthesized by the solid-phase method: [Phe2, Gly4]-beta h-EP(I), [Tyr5]-beta h-EP (II), and [Trp5[-beta h-ET (III). Analogs I and II are related to the highly potent hybrid analog [dermorphin1-7]-beta c-EP (beta c-EP). Radio-receptor-binding and analgesic assays gave relative potencies as follows, respectively: beta h-FP, 100, 100; I, 51, 43; II, 64, 30; III, 15, 4. The high potency of [dermorphin 1-7]-beta c-EP is not due to any one of the following structural elements: D-Ala2, Phe3-Gly4, Tyr5, and Pro6. Increasing hydrophobicity in position 5 (Met in beta-EP) leads to decreasing biological activity.

Amino Acid Sequence↗
PubMed1984

Human beta-endorphin. Synthesis and biological activity of analogs with modification in residue positions 8, 27, and 9 or 11.

Three analogs of human beta-endorphin (beta h-ER) were synthesized by the solid-phase method: [Gln8,Trp27]-beta h-EP (I), [Gln8,Arg9,Trp27]-beta h-EP (II), and [Gln9,Arg11,Trp27]-beta h-EP (III). Radioreceptor binding assay with use of tritiated beta h-EP as primary ligand gave relative potencies as follows: beta h-EP, 100;I, 778;II, 467;III, 449. Relative potencies in an analgesic assay were: beta h-EP, 100;I, 114;II, 165;III, 83. The 8-11 segment of beta h-EP can tolerate a net increase in charge of +2 without diminishing analgesic potency. The substitution of Glu8 may be one of the more dependable means of designing beta-endorphin antagonists.

Amino Acid Sequence↗
PubMed1983

Total synthesis of insulin-like growth factor I (somatomedin C).

Human insulin-like growth factor I (somatomedin C) with 70 amino acid residues and three disulfide bridges has been synthesized by the solid-phase method. The synthetic product behaves as a pure polypeptide in paper electrophoresis, isoelectric focusing, and high-performance liquid chromatography, Its elution behavior in Sephadex G-50, isoelectric point, amino acid composition, and growth-stimulating activity in bovine adrenal cortical cells or granulosa cells are comparable to those reported for the natural product. In radioimmunoassay, the synthetic product is indistinguishable from the natural hormone when either synthetic or natural product is used as the labeled ligand.

Adrenal Cortex↗
PubMed1983

High-performance partition chromatography of peptides on a new cross-linked agarose.

A new cross-linked agarose in bead form (20-40 microns in diameter) has been used for partition chromatography in two-phase solvent systems to give columns exhibiting efficiencies of several thousand theoretical plates. The efficiency of this high-performance partition column (70-80 plates per cm) far exceeds that of the most commonly used soft gel Sephadex G-50 (10 plates per cm). The column is operated under moderate pressure (5 p.s.i.) and can be regenerated. The new procedure appears capable of separating a peptide of moderate size, such as beta-endorphin (31 residues), from the majority of possible single-deletion sequences.

Animals↗
PubMed1983

Synthesis and properties of dermorphin and an analog of beta-endorphin containing the dermorphin sequence.

Dermorphin (I) and [D-Ala2, Phe3, Gly4, Tyr5, Pro6]-beta c-EP (II) have been synthesized by the solid-phase method (beta c-EP, camel beta-endorphin). Positions 1 through 7 of II correspond to the sequence of I. Relative potencies of synthetic peptides in the mouse tail-flick test for analgesia by the intracerebroventricular route were: human beta-endorphin, 100; camel beta-endorphin, 164; I, 450; II, 440. The dermorphin was about 670 times more potent than morphine in the assay. Peptide II represents a rare instance where the enkephalin moiety of beta-endorphin has been altered to produce a more potent analgesic.

Amino Acid Sequence↗
PubMed1983

Synthesis and properties of beta h-endorphin analogs containing the dynorphin-(1-13) sequence.

Two analogs of beta h-endorphin containing dynorphin-(5-13) or dynorphin-(6-13) sequence have been synthesized by the solid-phase method. Biological activities of the analogs have also been investigated. It was found that the opiate activity is about three times more than beta h-endorphin in the guinea pig ileum assay. Both analgesic potency and opiate receptor-binding activity of the analogs are lower when compared with beta h-endorphin. However, the analogs have interesting behavioral effects in mice.

Analgesics↗
PubMed1983

Enkephalin analogs: synthesis and properties of analogs with lipophilic or extended carboxyl-terminus. Quantitative structure-activity relationship of analogs modified in residue position 5.

Four analogs of enkephalin (EK) have been synthesized by the solid-phase method and their biological activities have also been investigated. All four analogs were less active than Met-enkephalin (Met-EK) as shown by relative potencies in the guinea pig ileum (GPI) assay: Met-EK, 100; [Phe5]-EK-NH2, 59; [Trp5]-EK-NH2, 11; Met-EK-Cys(Cam)-OH, 37; and N,N'-bis(Met-EK)-cystine, 34. Two of the analogs were more potent than Met-EK as shown by relative potencies in the mouse tail-flick assay for analgesia: Met-EK, 100; [Phe5]-EK-NH2, 1340; [Trp5]-EK-NH2, 1640. Quantitative structure-activity relationship calculations were carried out for GPI potencies of analogs substituted in position 5. The calculation indicated that, in this position, the bulkiness had the main influence.

Analgesics↗