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C A Slaughter

Publications and source records attributed to C A Slaughter.

114 records · Page 7Linked to original sources
PubMed1976

Evidence for the assignment of the loci AK1, AK3 and ACONs to chromosome 9 in man.

The segregation of human enzymes and chromosomes has been studied in more than 30 independent primary human-rodent somatic cell hybrids and a series of 64 subclones. The results strongly suggest that the locus determining AK1, 'red cell' adenylate kinase, is on chromosome 9 in man, and hence that the locus for the ABO blood groups and that for the Nail-patella syndrome may also be assigned to this chromosome. Evidence is presented indicating that another adenylate kinase, nucleoside triphosphate adenylate kinase, and also the soluble form of aconitase, are probably syntenic with AK1, and that the mitochondrial form of aconitase is probably not syntenic with these loci.

Aconitate Hydratase↗
PubMed1975

Aconitase polymorphism in man.

1. An electrophoretic method is described which resolves two groups of aconitase isozymes in human tissues, one group corresponding to the mitochondrial and the other to the soluble enzyme. This method has been used to screen human populations for electrophoretic variation. 2. Variant phenotypes of both the mitochondrial and the soluble aconitase are described, and family studies and sib-pair data demonstrate that the variation is genetically determined. 3. The variant isozyme patterns are accounted for in terms of allelic variation at two independent gene loci, ACONM and ACONS, which encode the mitochondrial and the soluble aconitase respectively. The electrophoretic survey has so far revealed two alleles at ACONM and seven alleles at ACONS. 4. The electrophoretic patterns shown by heterozygous individuals indicate that both soluble and mitochondrial aconitase are monomeric. The variant patterns also indicate that certain minor aconitase components resolved under the electrophoretic conditions employed represent 'secondary' isozymes of the primary translation products. 5. Population data on Europenas and Nigerians are presented and it is shown that both rare and common electrophoretic variants are segregating in the human species. The variation due to the three most common ACONS alleles in the Nigerians constitues a polymorphism.

Aconitate Hydratase↗
PubMedDate not supplied

Solid-phase synthesis of biologically active lipopeptides as analogs for spirochetal lipoproteins.

Bacterial lipoproteins, which are of particular interest because of their immunomodulatory activities, share a common N-terminal structural motif that consists of an N-acyl-S-diacylglyceryl cysteine residue. Synthetic tripalmitoylated analogs of the N-terminal sequences of several bacterial lipopetides have been found to reproduce the immunological activities of the corresponding intact lipoproteins. Methods for the synthesis of lipopeptide analogs of bacterial lipoproteins have hitherto relied upon the coupling of peptide moieties, lacking the N-terminal cystienyl residue, with a tripalmitoylglyceryl cysteine moiety synthesized separately in solution. A method is described here by which rapid and convenient synthesis of the entire lipopeptide is accomplished by solid-phase methods in which the N-terminal cysteinyl derivative is assembled stepwise while attached to the completed peptide moiety prior to cleavage from the resin. The method has been used to synthesize two lipohexapeptides representing the N-terminal sequences of the 47-kDa membrane lipoprotein of the syphilis spirochete, Treponema pallidum, and the outer surface protein A (OspA) of the Lyme disease spirochete, Borrelia burgdorferi. These lipopeptides, which were synthesized without detectable endotoxin contamination, exhibit macrophage-stimulating activity that is not expressed by the corresponding non-acylated hexapeptides. The data indicate that synthetic lipopeptides based on spirochetal lipoproteins are appropriate substitutes for the intact lipoproteins in immunological studies.

Amino Acid Sequence↗