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Biomedical subjects

C Yang

Publications and source records attributed to C Yang.

At least 523 records · Page 29Linked to original sources
PubMed1979

Thrombotic thrombocytopenic purpura in early pregnancy. Remission after plasma exchange.

A 24-year-old Chinese female developed fever, fluctuating neurological and renal manifestations, microangopathic hemolytic anemia, and thrombocytopenia during the 11th week of her first pregnancy. Therapy for thrombotic thrombocytopenic purpura (TTP), initiated during the 15th week of her pregnancy, including corticosteroids, platelet aggregation inhibitors, hysterotomy, and splenectomy was ineffective. However, dramatic improvement and remission occurred after plasma exchange of 3,560 ml was performed with the Haemonetics Model 30 Blood Cell Separator.

Adrenal Cortex Hormones↗
PubMed1979

[Rule of antibody structure. Primary structure of a human monoclonal IgAl-immunoglobulin (myeloma protein Tro). VI. Amino acid sequence of the L-chain, lambda-type, subgroup II].

The primary structure of the L-chain of an IgA1-immunoglobulin (Myeloma protein Tro) has been determined by means of cleavage with trypsin and, if necessary, with alpha-chymotrypsin. The tryptic peptides of the variable part were characterized by amino acid analysis, Dansyl-Edman degradation and cleavage with carboxypeptidase; the peptides of the constant part were identified by amino acid analyses and determination of its N- and C-terminal residues. The sequence of the remaining amino acids and the arrangement of the peptides were established in homology to known structures. The protein comprises 216 amino acids. The homology of the variable part clearly characterizes it as belonging to subgroup II of lambda-chains. In positions 27a, b and c, there are the subgroup-specific additional residues and in position 96 is the characteristic deletion. The constant part of the chain is Kern- and Oz- which indicates that it has serine in position 154 and arginine in position 191.

Amino Acid Sequence↗
PubMed1979

[Rule of antibody structure. Primary structure of a human monoclonal IgA-immunoglobulin (myeloma protein Tro). VII. Purification and characterization of the disulfide bridges].

Myeloma Protein Tro has been isolated from the plasma of a myeloma patient. Monomeric IgA was separated from its polymer (by chromatography on Sephadex G-200). Both the forms were split with pepsin or cyanogen bromide and, if necessary, with thermolysin and subtilisin. The cystin-containing peptides were isolated from the hydrolysates by chromatography on Sephadex, ion-exchange columns, preparative paper chromatography, thin-layer chromatography, electrophoresis or by a combination of these methods. They were characterized by amino acid analyses and by determination of the N-terminal amino acids using the Dansyl-Edman procedure. Thus all the disulfide bridges of an IgA1 immunoglobulin could be established. The monomer has all together 48 cysteins, seven in each L- and seventeen in each H-chain; all these are covalently bonded by SS-bridges. Free SH-groups were not detected. The J-chain could only be identified serologically in the polymeric form of the protein. It is shown that the subunits of the polymers are covalently attached through either Cysl3, Cysl7 or both these residues of the H-chain.

Amino Acid Sequence↗
PubMed1979

[The separation of the 4-[4-(dimethylamino) phenylazo]phenylthiohydantoin derivatives of leucine and isoleucine on polyamid thin-layer sheets in the picomol range (author's transl)].

The separation of the 4-[4-(dimethylamino)-phenylazo]phenylthiohydantoin derivatives of leucine and isoleucine has so far not been possible. In this paper a method is described which separates these two amino acid derivates in the picomol range on polyamide thin-layer sheets. The system (10% formic acid/ethanol 10:9) can be used either in one or in two dimensions.

Chromatography, Thin Layer↗
PubMed1974

Effect of endotoxin on tumor resistance in mice.

As reported earlier, an intraperitoneal injection of 1 mug of endotoxin (ET) from Serratia marcescens rendered mice resistant against the nonspecific mouse ascites tumor TA3-Ha upon challenge 24 h after pretreatment with ET. Further studies were aimed at the elaboration of conditions which achieved maximal resistance. It appears that (i) a 10-mug dose of ET was approximately the optimal dose for protection; (ii) pretreatment with ET 3 to 0 days prior to tumor challenge gave best protection; and (iii) the intravenous injection of ET showed a lower protection against the tumor than intraperitoneal application. Studies on the mechanism of ET protection indicate that (i) ET does not have a direct cytotoxic effect on tumor cells; (ii) normal spleen cells exposed to ET in vitro can adoptively transfer protection against tumor; and (iii) spleen cells activated in vivo by intravenous injection of ET can adoptively transfer protection. The possible involvement of mononuclear cells is discussed.

Animals↗
PubMed1967

Characterization and stability of ribosomes from mesophilic and thermophilic bacteria.

Ribosomes were isolated from three mesophilic and three thermophilic strains of Bacillus. The ribosomes consisted of about 55% protein and 45% ribonucleic acid. Average ratios for the absorbance at 260/235 and 260/280 mmu were 1.77 and 1.92 for the mesophiles and 1.63 and 1.84 for the thermophiles. Ultracentrifugation revealed mainly components with sedimentation coefficients of about 30, 50, 70, 100, and 120S. All the preparations were shown to contain a ribonuclease which, in the presence of ethylenediaminetetraacetic acid, led to ribosome breakdown as measured by the increase in acid-soluble nucleotides. The stability of the ribosomes from the thermophiles was consistently greater than that of the ribosomes from the mesophiles. After 5 hr at 37 C, the breakdown was about 80% for the ribosomes from the mesophiles and 55 to 70% for those from the thermophiles. At 60 C, the ribosomes from the mesophiles were broken down slightly more and at a faster rate than those from the thermophiles. At temperatures above 60 C, the breakdown was again more pronounced for the ribosomes from the mesophiles.

Bacillus↗