scholarly journals Characterization of rat spleen prostaglandin H d-isomerase as a sigma-class GSH transferase

1995 ◽  
Vol 311 (3) ◽  
pp. 739-742 ◽  
Author(s):  
D J Meyer ◽  
M Thomas
Keyword(s):  
Amino Acid ◽  
Simple Procedure ◽  
High Specificity ◽  
Strong Relationship ◽  
Prostaglandin Synthesis ◽  
Partial Amino Acid Sequence ◽  
Parasitic Helminths ◽  
Accessory Cells ◽  
Prostaglandin H

The prostaglandin H D-isomerase of rat immune accessory cells has been purified from spleen by a simple procedure, and its high specificity and activity [Urade, Fujimoto, Ujihara and Hayaishi (1987) J. Biol. Chem. 262, 3820-3825] have been confirmed in an assay coupled to prostaglandin H synthase. The enzyme also decreases the formation of 12[S]-hydroxy-5,8,10-heptadecatrienoic acid formed by the synthase in the presence of GSH and increases the overall rate of arachidonate oxidation. A partial amino acid sequence shows a strong relationship to GSH transferases of parasitic helminths and molluscs, indicating that it is the first example of a vertebrate sigma-class GSH transferase, and suggesting that certain helminth GSH transferases may be involved in prostaglandin synthesis.

scholarly journals Purification and characterization of prostaglandin-H E-isomerase, a sigma-class glutathione S-transferase, from Ascaridia galli

1996 ◽  
Vol 313 (1) ◽  
pp. 223-227 ◽  
Author(s):  
David J. MEYER ◽  
Richmond MUIMO ◽  
Michael THOMAS ◽  
David COATES ◽  
R. Elwyn ISAAC
Keyword(s):  
Parasitic Nematode ◽  
Helminth Parasites ◽  
Ascaridia Galli ◽  
Glutathione S Transferase ◽  
Purification And Characterization ◽  
Parasitic Helminths ◽  
Accessory Cells ◽  
Glutathione S Transferases ◽  
Prostaglandin H

Comparison of partial primary sequences of sigma-class glutathione S-transferases (GSH) of parasitic helminths and a GSH-dependent prostaglandin (PG)-H D-isomerase of rat immune accessory cells suggested that some of the helminth enzymes may also be involved in PG biosynthesis [Meyer and Thomas (1995) Biochem. J. 311, 739-742]. A soluble GSH transferase of the parasitic nematode Ascaridia galli has now been purified which shows high activity and specificity in the GSH-dependent isomerization of PGH to PGE, comparable to that of the rat spleen enzyme in its isomerization of PGH to PGD, and similarly stimulates the activity of prostaglandin H synthase. The enzyme subunit is structurally related to the rat spleen enzyme and sigma-class GSH transferases of helminths according to the partial primary sequence. The data support the hypothesis that some sigma-class GSH transferases of helminth parasites are involved in PG biosynthesis which, in the case of PGE, is likely to be associated with the subversion or suppression of host immunity. A PG-H E-isomerase of comparable specificity and activity has not previously been isolated.

Partial amino acid sequence and characterization of a new BmK AS-like polypeptide from Chinese scorpion

Toxicon ◽  
1997 ◽  
Vol 35 (4) ◽  
pp. 492-493
Author(s):  
Y. Liu ◽  
H.-M. Ren ◽  
Q. Hu ◽  
J. Zhao ◽  
B.-L. Song ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Partial Amino Acid Sequence

scholarly journals Characterization of collagenous and non-collagenous peptides of a glycoprotein isolated from alveoli of patients with alveolar proteinosis

1981 ◽  
Vol 193 (2) ◽  
pp. 447-457 ◽  
Author(s):  
S N Bhattacharyya
Keyword(s):  
Sialic Acid ◽  
Amino Acid ◽  
Polypeptide Chain ◽  
Proteolytic Enzymes ◽  
Lung Lavage ◽  
Sequence Analyses ◽  
Partial Amino Acid Sequence ◽  
Pepsin Digestion ◽  
Alveolar Proteinosis

A glycoprotein of Mr 62 000 was isolated from lung lavage material of patients with alveolar proteinosis. The glycoprotein was found to contain (per molecule) 72 residues of glycine, 5 residues of hydroxyproline, 3 molecules of sialic acid, 4.9 molecules of mannose, 4.0 molecules of galactose, 0.9 molecule of fucose and 7.0 molecules of N-acetylglucosamine. Limited pepsin digestion of the glycoprotein resulted in six peptides, three of which contained hydroxyproline and nearly 30% glycine, and two of which contained all the carbohydrate present in the glycoprotein of Mr 62 000. The three peptides containing hydroxyproline and with high content of glycine contained a repeating -Gly-X-Y-sequence in the peptide chain. Partial amino acid-sequence analyses on the peptides derived from the digestion of the alveolar glycoprotein with various proteolytic enzymes indicate that this glycoprotein is characterized by the presence of alternating collagenous and non-collagenous regions in the same polypeptide chain.

scholarly journals Characterization of Tbc2, a nucleus-encoded factor specifically required for translation of the chloroplast psbC mRNA in Chlamydomonas reinhardtii

2002 ◽  
Vol 157 (6) ◽  
pp. 953-962 ◽  
Author(s):  
Andrea H. Auchincloss ◽  
William Zerges ◽  
Karl Perron ◽  
Jacqueline Girard-Bascou ◽  
Jean-David Rochaix
Keyword(s):  
Zea Mays ◽  
Amino Acid ◽  
Chlamydomonas Reinhardtii ◽  
Amino Acid Sequence Identity ◽  
Middle Part ◽  
Phenotypic Characterization ◽  
Amino Acid Repeat ◽  
Partial Amino Acid Sequence ◽  
Sequence Identity

Genetic analysis has revealed that the three nucleus-encoded factors Tbc1, Tbc2, and Tbc3 are involved in the translation of the chloroplast psbC mRNA of the eukaryotic green alga Chlamydomonas reinhardtii. In this study we report the isolation and phenotypic characterization of two new tbc2 mutant alleles and their use for cloning and characterizing the Tbc2 gene by genomic complementation. TBC2 encodes a protein of 1,115 residues containing nine copies of a novel degenerate 38–40 amino acid repeat with a quasiconserved PPPEW motif near its COOH-terminal end. The middle part of the Tbc2 protein displays partial amino acid sequence identity with Crp1, a protein from Zea mays that is implicated in the processing and translation of the chloroplast petA and petD RNAs. The Tbc2 protein is enriched in chloroplast stromal subfractions and is associated with a 400-kD protein complex that appears to play a role in the translation of specifically the psbC mRNA.

PURIFICATION AND PARTIAL CHEMICAL CHARACTERIZATION OF SHEEP NEUROPHYSIN

1973 ◽  
Vol 74 (2) ◽  
pp. 226-236 ◽  
Author(s):  
Michel Chrétien ◽  
Claude Gilardeau
Keyword(s):  
Amino Acid ◽  
Polyacrylamide Gel Electrophoresis ◽  
Chemical Characterization ◽  
Terminal Amino Acid ◽  
Amino Acid Determination ◽  
Pituitary Glands ◽  
Terminal Amino ◽  
Partial Chemical ◽  
Acid Determination

ABSTRACT A protein isolated from ovine pituitary glands has been purified, and its homogeneity assessed by NH2- and COOH-terminal amino acid determination, ultracentrifugation studies, and polyacrylamide gel electrophoresis after carboxymethylation. Its chemical and immunochemical properties are closely similar to those of beef and pork neurophysins, less similar to those of human neurophysins. It contains no tryptophan (like other neurophysins) or histidine (like all except bovine neurophysin-I and human neurophysins). It has alanine at the NH2-terminus and valine at the COOH-terminus. Its amino acid composition is similar to, but not identical with those of porcine and bovine neurophysins.

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