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Biomedical subjects

J S Yang

Publications and source records attributed to J S Yang.

156 records · Page 9Linked to original sources
PubMed1974

Isoaccepting Transfer Ribonucleic Acids during Chilling Stress in Soybean Seedling Hypocotyls.

Total aminoacylation of glycine and leucine transfer RNAs was compared between chilled and nonchilled hypocotyls of 7-day-old soybean seedlings. Total charging was greater for both specific transfer RNAs from nonchilled sources. Isoaccepting transfer RNA species for glycine and leucine were fractionated using reverse phase column chromatography. Leucyltransfer RNAs were fractionated into six distinct fractions with relatively small shifts appearing in specific fractions between chilled and nonchilled sources. Glycyl-transfer RNAs were fractionated into two distinct fractions with major shifts appearing for both fractions between chilled and nonchilled sources.

Journal Article↗
PubMedDate not supplied

Degradation/solubilization of Chinese lignite by Penicillium sp. P6.

Penicillium sp. P6, isolated from coal mine soil at the Qiantong colliery Liaoning Province, Northwest China, can degrade Chinese lignite in 36 h on a plate colony and in 48 h using a 4-day cultured cell-free filtrate. Results of elemental analysis and IR spectrometry indicated that solubilized products exhibited some alterations in comparison to the original lignite. The amount of fulvic acid extracted from the biodegraded lignite was high, and the molecular distribution of the humic acids from biodegraded lignite changed distinctively in comparison to which extracted from the control lignite, possibly due to the depolymerization associated with fungal biodegradation.

Benzopyrans↗
PubMedDate not supplied

An anti-LFA-1 monoclonal antibody (LDA-8) induces cellular aggregation of human lymphoblastoid cell lines and peripheral blood lymphocytes.

The human leukocyte-function-associated antigen-1 (LFA-1) plays a key role in intercellular adhesion interactions of the immune response. A monoclonal antibody (mab), designated LDA-8, is described that recognizes LFA-1. In contrast to nearly all other anti-LFA-1 mabs, which inhibit cellular aggregation, LDA-8 induces cell-cell aggregation. The LDA-8 mab was generated by immunizing mice with membrane fragments from the Jurkat T-cell line. The LDA-8 mab stained peripheral blood mononuclear cells (PBMC), monocyte-depleted peripheral blood lymphocytes, purified monocytes, and a number of T and B tumor cell lines. The LDA-8 mab induced aggregation of PBMC from normal donors, as well as of cells from T-cell lines (MOLT4 and CEM). Control mabs directed against HLA class 1 or CD4 did not induce aggregation. Aggregation was concentration- and time-dependent. EDTA added to the cultures 1 hour prior to or together with the LDA-8 mab did not inhibit LDA-8-induced aggregate formation. Anti LFA-1 alpha-chain mab added to the cells 1 hour prior to LDA-8 mab, or together with the LDA-8 mab, also did not inhibit LDA-8-induced aggregation. In contrast, anti-LFA-1 beta-chain mab, added to the cells together with or 1 hour prior to the LDA-8 mab, significantly inhibited LDA-8-induced aggregate formation. The LDA-8 mab immunoprecipitated two polypeptide chains of 110 kDa and 160 kDa under non-reducing conditions and of 92 kDa and 162 kDa under reducing conditions, from cells of the MOLT-4 or CEM T-cell lines or phytohemagglutinin (PHA)-stimulated PBMC. The molecular mass of these polypeptides was identical to that of polypeptides immunoprecipitated by the anti-LFA-1 TS1.22 mab, suggesting that the LDA-8 mab and the anti-LFA-1 mab recognize the same molecule. This was confirmed by sequential immunoprecipitation. The LDA-8 mab recognizes a unique epitope on LFA-1 and induces cell aggregation that is blocked by mabs recognizing the beta-chain, but not the alpha-chain of the LDA-1 molecule.

Animals↗