scholarly journals Action of human cathepsin G on the oxidized B chain of insulin

1977 ◽  
Vol 161 (1) ◽  
pp. 17-19 ◽  
Author(s):  
A M J Blow ◽  
A J Barrett
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Human Neutrophil ◽  
Cathepsin G ◽  
British Library ◽  
Neutral Proteinase ◽  
Terminal Residue ◽  
Human Cathepsin ◽  
Chymotrypsin A

The specificity of cathepsin G, a serine neutral proteinase from human neutrophil leucotyes, was determine dby its action on the insulin B chain. The most susceptible bonds were Phe-24-Phe-25, Leu-15-Tyr-16 and Tyr-16-Leu-17. Other bonds hydrolysed were Leu-6-Cys(O3H)-7, Leu-11-Val-12, Leu-17-Val-18 and Phe-25-Tyr-26. These results suggest that the specificity of cathespin G is closer to that of pig chymotrypsin C than ox Chymotrypsin A. Tables listing amino acid composition, N-terminal residue, and yields of isolated peptides have been deposited as Supplementary Publication SUP 50 075 (8 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7B2, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1977) 161,1.

scholarly journals Action of human lysosomal elastase on the oxidized B chain of insulin

1977 ◽  
Vol 161 (1) ◽  
pp. 13-16 ◽  
Author(s):  
A M J Blow
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Human Neutrophil ◽  
British Library ◽  
Carboxyl Group ◽  
Pancreatic Elastase ◽  
Terminal Residue

The specificity of action of the lysosomal elastase of human neutrophil leucocytes on the oxidized B chain of insulin is similar to that of pig pancreatic elastase, but is more directed towards valine than alanine as the residue contributing the carboxyl group of the cleaved bond. The most susceptible bonds are Val-12-Glu-13 and Val-18-Cys(O3H)-19. Other bonds hydrolysed are Ala-14-Leu-15, Ser-9-His-10 and Cys, (O3H3)-7-Gly-8. Tables listing amino acid composition, N-terminal residue, and yields of isolated peptides have been deposited as Supplementary Publication SUP 50 075 (8 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1977) 161, 1.

scholarly journals The cDNA and protein sequences of human lactate dehydrogenase B

1987 ◽  
Vol 248 (3) ◽  
pp. 933-936 ◽  
Author(s):  
I Sakai ◽  
F S Sharief ◽  
Y C Pan ◽  
S S Li
Keyword(s):  
Amino Acid ◽  
Lactate Dehydrogenase ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Amino Acid Sequences ◽  
British Library ◽  
Amino Acid Residues ◽  
Coding Region ◽  
Cdna Insert ◽  
Protein Coding

Human lactate dehydrogenase B (LDH-B) cDNA was isolated and sequenced. The LDH-B cDNA insert consists of the protein-coding sequence (999 bp), the 5′ (54 bp) and 3′ (203 bp) non-coding regions, and the poly(A) tail (50 bp). The predicted sequence of 333 amino acid residues was confirmed by amino acid composition and/or sequence analyses of a total of 185 (56%) residues from tryptic peptides of human LDH-B protein. The nucleotide and amino acid sequences of the human LDH-B coding region show 68% and 75% homologies respectively with those of the human LDH-A. The peptide map and amino acid composition data have been deposited as Supplementary Publication SUP 50139 (7 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies are available on prepayment [see Biochem. J. (1987) 241, 5].

scholarly journals Purification and biochemical characterization of three major acidic proteins (BSP-A1, BSP-A2 and BSP-A3) from bovine seminal plasma

1987 ◽  
Vol 241 (3) ◽  
pp. 685-692 ◽  
Author(s):  
P Manjunath ◽  
M R Sairam
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Seminal Plasma ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Polyacrylamide Gel ◽  
Terminal Residue ◽  
Acidic Proteins

Three major acidic proteins of bovine seminal plasma, BSP-A1, BSP-A2 and BSP-A3, were purified to homogeneity, by employing fast protein liquid chromatography, gel filtration and h.p.l.c. The proteins were purified on the basis of their stimulatory effect on the basal release of gonadotropins by rat anterior-pituitary cells in culture. All three proteins migrated as distinct single bands in the presence or absence of 2-mercaptoethanol in SDS/polyacrylamide-gel electrophoresis. Their Mr values were estimated to be between 15,000 and 16,500 by SDS/polyacrylamide-gel electrophoresis. Similar Mr estimates were obtained when they were subjected to gel filtration on a calibrated column of Sephadex G-75 equilibrated in 0.05 M-acetic acid, pH 3.0. However, BSP-A1 and BSP-A2 were eluted as aggregated molecules (Mr 60,000-120,000) during gel filtration on Sephadex G-200 equilibrated in 0.05 M-NH4HCO3, pH 8.5, or phosphate buffer, pH 7.0, containing 0.15 M-NaCl. In the presence of 8 M-urea both BSP-A1 and BSP-A2 were eluted at positions corresponding to Mr values of 17,000-20,000. BSP-A1 and BSP-A2 had an identical amino acid composition, which differed largely from that of BSP-A3. All three proteins contained aspartic acid as the N-terminal residue, and cysteine was identified as the C-terminal residue. BSP-A1 and BSP-A2 are glycoproteins containing galactosamine, sialic acid and neutral sugars, but BSP-A3 did not contain any covalently attached sugars. Whereas BSP-A2 and BSP-A3 were eluted unadsorbed, BSP-A1 bound to wheat-germ lectin-Sepharose 6MB and could be eluted by the competing sugar N-acetyl-D-glucosamine. Treatment of BSP-A1 and BSP-A2 with trypsin resulted in complete loss of gonadotropin-release activity, but BSP-A3 retained full activity. Antibody raised against BSP-A1 did not cross-react with BSP-A3, or vice versa. All these properties indicated marked structural differences between BSP-A3 and BSP-A1 (or BSP-A2). On the basis of amino acid composition it was concluded that BSP-A1, BSP-A2 and BSP-A3 are the same as the gonadostatins [Esch, Ling, Bohlen, Ying & Guillemin (1983) Biochem. Biophys. Res. Commun. 113, 861-867].

scholarly journals Purification and properties of a proteolytic enzyme from the cercariae of the human trematode parasite Schistosoma mansoni

1982 ◽  
Vol 201 (1) ◽  
pp. 137-144 ◽  
Author(s):  
W J Landsperger ◽  
M A Stirewalt ◽  
M H Dresden
Keyword(s):  
Amino Acid ◽  
Schistosoma Mansoni ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Isoelectric Point ◽  
Proteolytic Enzymes ◽  
Sodium Dodecyl ◽  
Skin Penetration ◽  
Cathepsin G ◽  
Trematode Parasite

Skin penetration by the cercarial stage of the human trematode parasite Schistosoma mansoni is mediated by the secretion of proteolytic enzymes able to digest components of mammalian connective tissues. In the present study the purification of these proteinases from cercarial homogenates is reported. The major proteinase species has a mol. wt. of approx. 25 000 and exists in monomeric form as determined by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. This proteinase has an isoelectric point of 6.0. Studies presented here, with a variety of substrates and inhibitors, confirm previous claims that these proteinases belong to the serine class, and, in addition, suggest that they resemble the vertebrate chymotrypsins rather than trypsins or elastases. However, the amino acid composition of the cercarial proteinase differs significantly from bovine chymotrypsin and from the human leucocyte chymotrypsin-like cathepsin G. The amino-acid-composition differences between these proteinases are consistent with their differences in isoelectric point. In order to obtain an insight into the role of the proteinase in skin penetration, its activity on cartilage proteoglycan monomers and on the isolated peptide backbone of proteoglycan was studied. The results of the present study indicate that the cercarial enzyme catalyses a limited specific digestion of the peptide core.

Human pituitary thyrotropin. Isolation and characterization of the hormone and its subunits

1977 ◽  
Vol 55 (7) ◽  
pp. 747-754 ◽  
Author(s):  
M. R. Sairam ◽  
Choh Hao Li
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Disc Electrophoresis ◽  
Carbohydrate Content ◽  
Human Pituitary ◽  
Terminal Residue ◽  
Isolation And Characterization

Procedures have been described for the isolation of highly purified thyrotropin from frozen or acetone-preserved glands or from side fractions of somatotropin isolation and for the separation of its α and β subunits. The products have been characterized by terminal residue analyses, amino acid composition, carbohydrate content, disc electrophoresis, ultracentrifugation, and biological activity.

Conversion of Pig Prothrombin into Thrombin: Amino Acid Composition of the Active Enzyme

1974 ◽  
Vol 52 (4) ◽  
pp. 336-344 ◽  
Author(s):  
Antonio Rossi ◽  
José Roberto Giglio
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Column Chromatography ◽  
Active Enzyme ◽  
Terminal Residue

Preparation and activation of partially purified pig prothrombin are described. The enzyme, after column chromatography in Amberlite IRC-50, showed alanine as the N-terminal residue and an [Formula: see text] of 1.50 at pH 7.0 and 280 nm.The amino acid composition of pig thrombin is reported and compared with that of bovine origin. Pig thrombin showed 1.0 mol of isoleucine to 0.6 mol of threonine as N-terminals.The effects of storage of pig prothrombin are discussed.

Effect of maternal diet on the amino acid composition of human uterine fluid

2014 ◽  
Author(s):  
Alexandra Jayne Kermack ◽  
Ying Cheong ◽  
Nick Brook ◽  
Nick Macklon ◽  
Franchesca D Houghton
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Maternal Diet ◽  
Uterine Fluid
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