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Biomedical subjects

D Chung

Publications and source records attributed to D Chung.

At least 73 records · Page 4Linked to original sources
PubMed1987

An accurate method of 192Ir wire implantation for locally advanced carcinoma of breast.

An accurate and reproducible method of 192Ir wire implantation of locally advanced breast tumour after locoregional megavoltage external radiotherapy has been described. The method includes the use of cobex cast for breast and tumour immobilization, of computed tomography for tumour localization, of computer for planning and isodose display and of specially made template to guide insertion of trocars and 192Ir wires.

Brachytherapy↗
PubMed1986

The primary structure of monkey pituitary growth hormone.

Monkey growth hormone (MGH) has been purified by reverse-phase high-performance liquid chromatography (HPLC). Tryptic digests of MGH were separated by HPLC and paper electrophoresis. From amino acid composition, from NH2-terminal residue and sequence analyses of these tryptic peptides, and from their alignment with those of human growth hormone, the primary structure of MGH was proposed. There are only four residues which are different in these two growth hormone molecules.

Amino Acid Sequence↗
PubMed1985

Human seminal alpha inhibins: isolation, characterization, and structure.

Two additional peptides with inhibin-like activity have been isolated from human seminal plasma. One consists of 52 amino acids and the other, 92 amino acids. They are designated alpha-inhibin-52 and alpha-inhibin-92. Sequence analyses show that the NH2-terminal 31 amino acids of alpha-inhibin-52 are identical to the structure of the inhibin-like peptide previously reported [ILP-(1-31), now designated alpha-inhibin-31], and the COOH-terminal 52 amino acids of alpha-inhibin-92 are identical to the structure of alpha-inhibin-52. The amino acid sequence of alpha-inhibin-92 is: (sequence in text) Bioassay data in mouse pituitaries in vitro show that alpha-inhibin-52 is 3.4 times more active and alpha-inhibin-92 is greater than 40 times more active than alpha-inhibin-31 in suppressing follitropin-release. Radioimmunoassay data indicate that alpha-inhibin-52 and alpha-inhibin-92 have only 60% immunoreactivity.

Amino Acid Sequence↗
PubMed1985

Evidence for the existence of [Gln9]-beta-lipotropin in human pituitary glands.

The isolation of two peptides similar in amino acid composition to that of human beta-lipotropin is presented. Peptide patterns after enzymatic digestions of these two peptides by Staphylococcus aureus protease and by trypsin were nearly identical. Paper electrophoresis and amino acid analyses of acidic peptides generated from the enzymatic digestions of these two peptides indicate that there is an amide difference between the two peptides. It is proposed that this amide difference is in amino acid residue number nine, and that one is the human beta-lipotropin and the other its [Gln9] analog.

Amino Acid Sequence↗
PubMed1985

Distinct behavior of beta-endorphin and corticotropin toward leucine aminopeptidase action.

Reactions of human beta-endorphin, corticotropin and their synthetic analogs with leucine aminopeptidase have been investigated. The results confirmed previous findings that beta-endorphin is resistant to the aminopeptidase action whereas corticotropin is not. Beta-endorphin-(1-5) is completely digested by the enzyme while beta-endorphin-(1-17) is resistant. In contrast, the NH2-terminal 7 residues in corticotropin are removed readily by leucine aminopeptidase. This is confirmed by the observation that human corticotropin-(7-38) is not hydrolyzed by the enzyme. This contrasting behavior of the two hormones toward leucine aminopeptidase may be related to differences in their conformational structures.

Adrenocorticotropic Hormone↗
PubMed1983

Studies on prolactin 48: isolation and properties of the hormone from horse pituitary glands.

Isolation of prolactin from equine pituitary glands has been described. It has a potency of 42 IU/mg in the pigeon crop-sac test and consists of 199 amino acids. The hormone has only four half-cystine residues in contrast to other mammalian prolactins which have six residues. From NH2-terminal sequence analysis and amino acid composition of cyanogen bromide fragments, the NH2-terminal disulfide loop is missing in the equine prolactin molecule. Circular dichroism spectra indicate that the alpha-helical content of equine prolactin appears to be lower (50%) than that found in the ovine hormone (65%).

Amino Acids↗
PubMed1983

Isolation of pancreatic trypsin inhibitor from bovine pituitary glands.

A trypsin inhibitor has been isolated from bovine pituitary extracts. From its amino acid composition, NH2-terminal residue, mobility in paper electrophoresis, and behavior in high-performance liquid chromatography and from the tryptic pattern of the performic acid-oxidized material, it appears that the inhibitor is identical to the Kunitz and Northrop pancreatic trypsin inhibitor.

Amino Acids↗
PubMed1982

Isolation and properties of beta-endorphin-(1-27)-like peptide from bovine brains.

A beta-endorphin-(1-27)-like peptide was isolated from bovine cerebral hemisphere extracts by gel filtration, ion-exchange chromatography, high performance liquid chromatography and paper electrophoresis. The peptide had tyrosine as the amino-terminal residue and its amino acid composition was nearly identical to that of equine pituitary beta-EP-(1-27). It had also the same mobility as equine pituitary beta-EP-(1-27) in paper electrophoresis. In radioimmunoassay and opiate receptor-binding assay, the brain peptide had 50% activity when compared with human beta-endorphin-(1-27). Evidence for the occurrence of NH2-acetylated form of beta-endorphin-(1-27) is also presented.

Animals↗
PubMed1981

Isolation, characterization and amino acid sequence of beta-lipotropin from human pituitary glands.

Beta-Lipotropin has been purified to homogeneity from human pituitary glands. It consists of 89 amino acids with a molecular weight of 11 700. The lipolytic potency of the human hormone is identical to that of ovine beta-LPH. The amino acid sequence has been determined as follows: (see formula in text). When compared with the structure of the ovine hormone, the sequence at the NH2-terminal 33 residues exhibits considerable variability.

Amino Acid Sequence↗
PubMed1981

beta-Lipotropin: primary structure of the hormone from the ostrich pituitary gland.

The amino acid sequence of beta-lipotropin from the ostrich pituitary has been determined. It consists of 79 amino acids. The amino acid sequence has been determined as follows: H-(1)AlA-Leu-Pro-Pro-Ala-Ala-Met-Leu-Pro-(10)Ala-Ala-Ala-Glu-Glu-Glu-Glu-Gly-Gl u-Glu-(20)Glu-Glu-Glu-Gly-Glu-Ala-Glu-Lys-Glu-Asp-(30)Gly-Gly-Ser-Tyr-Arg-Met-A rg-His-Phe-Arg-(40)Trp-Gln-Ala-Pro-Leu-Lys-Asp-Lys-Arg-Tyr-(50)Gly-Gly-Phe-Met- Ser-Ser-Glu-Arg-Gly-Arg-(60)Ala-Pro-Leu-Val-Thr-Leu-Phe-Lys-Asn-Ala-(70)Ile-Val -Lys-Ser-Ala-Tyr-Lys-Lys-Gly-(79)Gln-OH. When compared with the primary structures of other known beta-lipotropins, the sequence at the NH2-terminal, beta-melanotropin and beta-endorphin portions of the molecule exhibit considerable variability.

Amino Acid Sequence↗
PubMed1981

beta-Endorphin: isolation, amino acid sequence and synthesis of the hormone from horse pituitary glands.

Beta-endorphin has been isolated from equine pituitaries. Its amino acid sequence is identical to that of ovine, bovine and camel beta-endorphins except for substitution of the threonine residue at position 6 by serine. The equine beta-endorphin has also been synthesized by the solid-phase method. In comparison with the human hormone, equine beta-endorphin was shown to possess 3 times the receptor-binding activity in rat membrane preparations and 1.6 times the analgesic potency in the mouse tail-flick assay.

Amino Acid Sequence↗
PubMed1981

Carnitine in the perinatal metabolism of lipids. I. Relationship between maternal and fetal plasma levels of carnitine and acylcarnitines.

Since premature infants have a limited capacity for fatty acid oxidation, supplementation with carnitine may improve their utilization of fat. Documentation of the source and extent of fetal carnitine reserves should explain the possible need for exogenous carnitine in the neonate. Correlation between free carnitine concentration in maternal and umbilical arterial plasma at birth (r = .45, P less than .01) indicates that the initial concentration of free carnitine in the newborn depends on the maternal level. Thin-layer chromatography shows more gamma-butyrobetaine in maternal than umbilical arterial plasma indicating higher availability of the precursor of carnitine biosynthesis. Elevated fatty acid oxidation in maternal tissues seems to be reflected by larger amounts of long-chain acylcarnitines in maternal plasma. Short-chain acylcarnitines, mainly acetylcarnitine, are higher in the umbilical vein than in maternal plasma (P less than .01) indicating that the conceptus (the placenta or fetus) is either producing more or utilizing less acetylcarnitine. Plasma levels of carnitine rapidly decrease in premature newborns during the first three days after birth if no exogenous carnitine is given (P less than .001), while no significant changes of total carnitine were detected in adult patients on total parenteral alimentation for one week. This difference indicates lower carnitine depots or limited capacity for carnitine biosynthesis in neonates. The possibility still requires further investigation that the development of the optimal rate of fatty acid oxidation in human newborns, as well as in other newborn mammals, may depend on the supply of exogenous carnitine.

Carnitine↗