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Biomedical subjects

S Brenner

Publications and source records attributed to S Brenner.

At least 325 records · Page 18Linked to original sources
PubMed1986

Macrophage migration inhibition factor in pemphigus vulgaris.

Three cases of pemphigus vulgaris probably induced by ampicillin treatment are described. All of the patients' lymphocytes responded positively toward ampicillin in the migration inhibition factor test. There is a possibility that this test might be significant in recognizing the offending drug in vitro.

Ampicillin↗
PubMed1986

Toward a physical map of the genome of the nematode Caenorhabditis elegans.

A technique for digital characterization and comparison of DNA fragments, using restriction enzymes, is described. The technique is being applied to fragments from the nematode Caenorhabditis elegans (i) to facilitate cross-indexing of clones emanating from different laboratories and (ii) to construct a physical map of the genome. Eight hundred sixty clusters of clones, from 35 to 350 kilobases long and totaling about 60% of the genome, have been characterized.

Journal Article↗
PubMed1986

A survey of patient and family satisfaction with social work services.

Client satisfaction can be important indicator of the quality of social work services. This article reports the results of a survey conducted by a social work department of a large urban teaching hospital to elicit patient and family reaction to its services. A random, proportionate sample of in- and out-patient cases in medical and psychiatric programs was used. In general, staff was seen as helpful, although with interesting variations depending on the social work function performed. The findings have implications for education, supervision, quality assurance, levels of staffing and staff's perception of their usefulness.

Attitude of Health Personnel↗
PubMed1985

Cloning of the gene encoding the hydrogenase from Desulfovibrio vulgaris (Hildenborough) and determination of the NH2-terminal sequence.

The gene encoding the hydrogenase from Desulfovibrio vulgaris (Hildenborough) has been cloned in Escherichia coli. D. vulgaris DNA was digested with the restriction endonucleases EcoRI and SalI and ligated into the vector pUC9 [Vieira, J. & Messing, J. (1982) Gene 19, 259-268], which had been cut with these same enzymes. Approximately 9000 recombinant clones were obtained by transformation of E. coli JM 101 followed by growth on rich plates with ampicillin for selection and isopropyl-beta-D-thiogalactoside and 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside present for detection of recombinants. The recombinant clones were then screened for production of immunoreactive proteins with rabbit antisera against purified hydrogenase and 125I-labelled protein A. 28 positive clones were found in this initial screening. These were further tested in an immunocompetition experiment, which showed that the protein product from one clone behaved identically to purified hydrogenase. The plasmid pHV15 isolated from this clone has a 4.7 X 10(3)-base-pair SalI/EcoRI insert. Cells of E. coli JM 101 transformed with pHV 15 produce a hydrogenase polypeptide of molecular mass 46 kDa as detected by Western blotting. The mass, as well as the Cleveland mapping pattern of the polypeptide produced by E. coli, are identical with those of the hydrogenase isolated from D. vulgaris (Hildenborough). Southern blotting of restriction-enzyme-digested D. vulgaris DNA, using the nick-translated 4.7 X 10(3)-base-pair SalI/EcoRI fragment as a probe, indicates the presence of a single gene with an internal PstI site. The NH2-terminal sequence of the hydrogenase was determined to be: (sequence in text). This information should allow an unambiguous identification of the hydrogenase gene.

Amino Acids↗
PubMed1985

Nucleotide sequence of the gene encoding the hydrogenase from Desulfovibrio vulgaris (Hildenborough).

The nucleotide sequence of the 4.7-kb SalI/EcoRI insert of plasmid pHV 15 containing the hydrogenase gene from Desulfovibrio vulgaris (Hildenborough) has been determined with the dideoxy chain-termination method. The structural gene for hydrogenase encodes a protein product of molecular mass 45820 Da. The NH2-terminal sequence of the enzyme deduced from the nucleic acid sequence corresponds exactly to the amino acid sequence determined by Edman degradation. The nucleic acid sequence indicates that a N-formylmethionine residue precedes the NH2-terminal amino acid Ser-1. There is no evidence for a leader sequence. The NH2-terminal part of the hydrogenase shows homology to the bacterial [8Fe-8S] ferredoxins. The sequence Cys-Ile-Xaa-Cys-Xaa-Xaa-Cys-Xaa-Xaa-Xaa-Cys-Pro-Xaa-Xaa-Ala-(Ile) occurs twice both in the hydrogenase and in [8Fe-8S] ferredoxins, where the Cys residues have been shown to coordinate two [4Fe-4S] clusters [Adman, E. T., Sieker, L. C. and Jensen, L. H. (1973) J. Biol. Chem. 248, 3987-3996]. These results, therefore, suggest that two electron-transferring ferredoxin-like [4Fe-4S] clusters are located in the NH2-terminal segment of the hydrogenase molecule. There are ten more Cys residues but it is not clear which four of these could participate in the formation of the third cluster, which is thought to be the hydrogen binding centre. Another gene, encoding a protein of molecular mass 13493 Da, was found immediately downstream from the gene for the 46-kDa hydrogenase. The nucleic acid sequence suggests that the hydrogenase and the 13.5-kDa protein belong to a single operon and are coordinately expressed. Since dodecylsulfate gel electrophoresis of purified hydrogenase indicates the presence of a 13.5-kDa polypeptide in addition to the 46-kDa component, it is proposed that the hydrogenase from D. vulgaris (Hildenborough) is a two-subunit enzyme.

Base Sequence↗
PubMed1985

An erythromycin-resistance gene from an erythromycin-producing strain of Arthrobacter sp.

A gene (ermA) coding for a presumed erythromycin-resistance (ErR) determinant from an Er-producing Arthrobacter sp. strain (NRRLB3381) was isolated from a gene bank in phage vector lambda 2001 by probing with a Streptomyces ErR gene. Strongly hybridizing fragments were subcloned and the appropriate segments sequenced. The ermA gene is 76 mol% G + C in content and specifies a protein of 340 aa with an Mr of 37454. S1 nuclease mapping and primer extension identified the putative promoter, which resembles the consensus sequence of Escherichia coli promoters particularly in the -10 region. A potential ribosome-binding site (RBS) (AGGAG) was also located. Unexpectedly, the majority of in vivo ermA transcripts detected were only 245 nt long, suggesting that expression of ErR may be regulated post-transcriptionally. Substantial homology is observed between the predicted aa sequences of the ermA-coded protein and the products of three other ErR determinants, from organisms that do not produce Er.

Arthrobacter↗
PubMed1985

Identical short peptide sequences in unrelated proteins can have different conformations: a testing ground for theories of immune recognition.

The ability of antibodies raised against disordered short peptides to interact frequently with their cognate sequences in intact folded proteins has raised a major theoretical issue in protein chemistry. We propose to address this issue by using antibodies raised against peptides with identical sequences, but different conformations, in pairs of unrelated proteins of known three-dimensional structure. The general search method presented here enabled us to detect candidate sequences for such immunological studies.

Animals↗
PubMed1985

Leukotrienes.

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Arachidonic Acid↗
PubMed1985

Familial pemphigus vulgaris.

A case of familial pemphigus vulgaris is described in an uncle and his niece who developed the disease 18 years apart. The man died from pemphigus in 1964. The diagnosis was confirmed histopathologically in both cases, but immunofluorescent microscopic studies were performed only in the woman because the technique was not available in 1964. HLA typing in the woman and her daughter and sister showed A 26, BW 38 and DRW 4 in all of them. Clinical disease did not develop in the other family members.

Female↗