The association of rapid volume expansion and intraventricular hemorrhage in the preterm infant.
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Cerebral Hemorrhage↗
Biomedical subjects
D Chung
Publications and source records attributed to D Chung.
Isolation and amino acid sequence of gamma-lipotropin from human pituitary glands.
gamma-Lipotropin has been purified to homogeneity from human pituitary glands. It consists of 56 amino acids with one residue each of Trp, Thr, Val, Tyr, and Phe. The amino acid sequence has been determined as follows: H-Glu-Leu-Thr-Gly-Gln-Arg-Leu-Arg-Gln-Gly-Asp-Gly-Pro-Asn-Ala-Gly-Ala-Asp-Asp-G ly-Pro-Gly-Ala-Gln-Ala-Asp-Leu-Glu-His-Ser-Leu-Leu-Val-Ala-Ala-Glu-Lys-Lys-Asp- Glu-Gly-Pro-Tyr-Arg-Met-Glu-His-Phe-Arg-Trp-Gly-Ser-Pro-Pro-Lys-Asp-OH. Comparison with the structure of the ovine and porcine hormones reveals that the 23-amino-acid sequence at the COOH terminus is highly conserved in evolution.
Amino Acid Sequence↗
Isolation and characterization of beta-lipotropin from fin whale pituitary glands.
The isolation and characterization of beta-lipotropin from fin whale (Balaenoptera physalus) pituitary glands are described. The proposed primary structure is also presented. Fin whale beta-LPH exhibited an identical lipolytic activity when compared with human hormone.
Amino Acid Sequence↗
Isolation and characterization of beta-lipotropin and adrenocorticotropin from turkey pituitary glands.
Beta-Lipotropin and corticotropin have been isolated in highly purified form from turkey pituitary glands. The isolated hormones were characterized by NH2-terminal residue, amino acid and sequence analyses. Their hormonal activity and immunoactivity were also investigated.
Adrenocorticotropic Hormone↗
Adrenocorticotropin 53. The amino acid sequence of the hormone from the ostrich pituitary gland.
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Adrenocorticotropic Hormone↗
Isolation, characterization, and synthesis of a corticotropin-inhibiting peptide from human pituitary glands.
A corticotropin-inhibiting peptide (CIP) has been isolated from human pituitary extracts. It consists of 32 amino acids with a proposed sequence identical to residues 7--38 of corticotropin (ACTH). The peptide has been synthesized by the solid-phase method. The melanotropic activity of the peptide is estimated to be 30% of the potency of ACTH. It is devoid of corticosteroidogenic activity but is able to inhibit ACTH-stimulated corticosterone production in isolated rat adrenal cells.
Adrenocorticotropic Hormone↗
Isolation, structure, synthesis and morphine-like activity of beta-endorphin from human pituitary glands.
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Amino Acid Sequence↗
Isolation and primary structure of beta-endrophin and beta-lipotropin from bovine pituitary glands.
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Amino Acid Sequence↗
beta-Endorphin: structure-activity relationships in the guinea pig ileum and opiate receptor binding assays.
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Animals↗
Isolation, characterization and opiate activity of beta-endorphin from human pituitary glands.
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Amino Acid Sequence↗
Primary structure of human beta-lipotropin.
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Amino Acid Sequence↗
Isolation and structure of an untriakontapeptide with opiate activity from camel pituitary glands.
The isolation of an untriakontapeptide from camel pituitary extracts has been described. Its structure has been determined and shown to be identical to the sequence of carboxyl-terminal 31 amino acids of ovine beta-lipotropin. The peptide possesses very low lipotropic activity but significant opiate activity.
Amino Acids↗
Isolation, characterization, and amino acid sequence of melanotropins from camel pituitary glands.
The isolation of two beta-melanotropins and two alpha-melanotropins from camel pituitary glands has been described, and their amino acid sequences have been determined. Two of them are identified as alpha-melanotropin and deacetylated alpha-melanotropin. There are also two beta-melanotropins whose structures are identical with the bovine hormone except that one has glycine in position 2 and the other glycine in position 2 as well as glutamine in position 8. The melanocyte-stimulating and lipolytic activities of these four camel melanotropins have been investigated by in vitro assay procedures.
Amino Acid Sequence↗
The primary structure of ovine interstitial cell stimulating hormone. IV: Disulfide bridges of the beta subunit.
The disulfide linkage of the 12 half-cystine residues in the beta subunit of ovine interstitial cell stimulating hormone has been investigated by enzymic and partial acid hydrolysis of the intact molecule. Results indicate that the disulfide bridges are formed by residues 9-38, 23-72, 26-110, 34-90, 57-88, and 93-100.
Amino Acid Sequence↗
Purification of antibodies to protein hormones by affinity chromatography on divinylsulfonyl sepharose.
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Animals↗
Amino acid sequence of human chorionic somatomammotropin.
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Amino Acid Sequence↗
The effect of haemodynamic changes on maximum acceleration in the anaesthetized dog.
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Acceleration↗
Primary structure of the human chorionic somatomammotropin (HCS) molecule.
The complete amino acid sequence of the human chorionic somatomammotropin molecule been proposed; and then compared with that of human growth hormone and ovine lactogenic hormone.
Amino Acid Sequence↗