Human Red Cell Peptidases

Lewis, William H.; Harris, Harry

doi:10.1038/215351a0

Cited by 280 publications

(79 citation statements)

References 4 publications

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“…The conditions of this assay were set according to published observations (16,(31)(32)(33). The standard assay was performed in a final volume of 100 l in plastic cuvettes with a 1-cm optical path (UVettes; Eppendorf).…”

Section: Methodsmentioning

confidence: 99%

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The Proteomics of N-terminal Methionine Cleavage

Frottin

Martinez

Peynot

et al. 2006

Molecular & Cellular Proteomics

344

350

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Section: Methodsmentioning

confidence: 99%

“…The only available test that appeared fully independent of the peptide sequence had only been used in a discontinuous manner. This assay involved coupling with two other activities, those of amino-acid oxidase and peroxidase (16,(31)(32)(33). We set up this assay for use in continuous conditions.…”

Section: Validation Of the Experimental In Vitromentioning

confidence: 99%

The Proteomics of N-terminal Methionine Cleavage

Frottin

Martinez

Peynot

et al. 2006

Molecular & Cellular Proteomics

344

350

View full text Add to dashboard Cite

“…The filters were then washed (20 min per wash with 0.1% NaDodSO4) as follows: apoE probe, twice in 2 x SSC and twice in 0.5 x SSC at 55°C; apoCII, twice in 2x SSC and twice in 0.5x SSC at 65°C; apoCI and C3, twice in 2x SSC Detter et al (40). Electrophoresis of PEPD (peptidase D, EC 3.4.13.9) was by the method of Lewis and Harris (41).…”

Section: Methodsmentioning

confidence: 99%

Regional mapping of human chromosome 19: organization of genes for plasma lipid transport (APOC1, -C2, and -E and LDLR) and the genes C3, PEPD, and GPI.

Lusis¹,

Heinzmann²,

Sparkes³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

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We report the regional mapping of human chromosome 19 genes for three apolipoproteins and a lipoprotein receptor as well as genes for three other markers. The regional mapping was made possible by the use of a reciprocal whole-arm translocation between the long arm of chromosome 19 and the short arm of chromosome 1. Examination of three separate somatic cell hybrids containing the long arm but not the short arm of chromosome 19 indicated that the genes for apolipoproteins CI, CII, and E (APOCI, APOC2, and APOE, respectively) and glucose-6-phosphate isomerase (GPI) reside on the long arm, whereas genes for the low density lipoprotein receptor (LDLR), complement component 3 (C3), and peptidase D (PEPD) reside on the short arm. When taken together with previous studies, our results suggest the following physical gene map: pter-LDLR-C3-pl3.2-PEPD-centromere-(APOE, APOCI, APOC2, GPI)-qter. In addition, we have isolated a single A phage carrying both APOCI and part ofAPOE. These genes are tandemly oriented and are separated by about 6 kilobases of genomic DNA. Since previous family studies indicate tight linkage of APOE and APOC2, the apolipoprotein genes APOCI, APOC2, and APOE form a tight complex on the long arm of chromosome 19, suggesting the possibility of coordinate regulation.

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“…The starch gel was sliced into two layers after electrophoresis. The reaction mixture, containing the peptide under examination, Lamino acid oxidase, horseradish peroxidase, o-dianisidine dihydrochloride, and MnCl2, was mixed with an equal volume of 2% aqueous agar (14), and poured over the sliced surface of the gel. The starch gel with its agar overlay was then incubated for 1 or 2 hr at 37°C.…”

Section: Methodsmentioning

confidence: 99%

“…Peptide hydrolase activities have also been reported in many tissues other than small intestinal mucosa, such as red blood cells and mouse ascites tumor cells, kidney, liver, and connective tissue, but they have not been examined for structural and functional similarities (12)(13)(14)(15).…”

Section: Introductionmentioning

confidence: 99%

Peptide hydrolases in the brush border and soluble fractions of small intestinal mucosa of rat and man

Kim¹,

Birtwhistle²,

Kim³

1972

J. Clin. Invest.

159

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A BST RA CT Peptide hydrolases, catalyzing the hydrolysis of 13 dipeptides and 5 tripeptides into their respective amino acids, were studied in small intestinal mucosa and other tissues, in man and in the rat.Studies on the subcellular distribution of these enzymes showed enzyme activities in both the soluble and brush border fractions of the rat small intestinal mucosa, the former constituting 80-90% and the latter 10-15% of the total activity. Zymogram studies of peptide hydrolases, in both fractions, yielded multiple bands indicating multiple zones of enzyme activity. With most substrates a rather broad range of enzyme activities was observed in the soluble fraction differing only slightly from substrate to substrate, the exception being when L-leucyl-L-proline was used: this latter led to a zymogram pattern which was quite distinct. The synthetic substrates, L-leucyl-P-naphthylamide and Lleucinamide appeared to be hydrolyzed by two electrophoretically distinct enzymes, different from those hydrolyzing other leucyl-containing peptide substrates.Zymogram patterns of the brush border membrane fraction were quite different from those of the soluble fraction of rat small intestine indicating that enzymes from the two sources may be different. No comparable human data were obtained.Peptide hydrolases in the soluble fractions of various organs from the same species gave similar zymogram patterns, while those from the plasma membrane-bound fractions of different organs in the same species were peculiar to each organ. From these data, it is suggested that peptide hydrolases in the brush border and the soluble fractions of small intestine are distinct enzymes and may play different roles in cellular function.

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Human Red Cell Peptidases

Cited by 280 publications

References 4 publications

The Proteomics of N-terminal Methionine Cleavage

The Proteomics of N-terminal Methionine Cleavage

Regional mapping of human chromosome 19: organization of genes for plasma lipid transport (APOC1, -C2, and -E and LDLR) and the genes C3, PEPD, and GPI.

Peptide hydrolases in the brush border and soluble fractions of small intestinal mucosa of rat and man

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