scholarly journals Proteinase inhibitors of bovine nasal cartilage

1978 ◽  
Vol 169 (3) ◽  
pp. 721-724 ◽  
Author(s):  
P J Roughley ◽  
G Murphy ◽  
A J Barrett
Keyword(s):  
Molecular Weight ◽  
Inhibitory Activity ◽  
Cathepsin B ◽  
Proteinase Inhibitors ◽  
Low Molecular Weight ◽  
Gel Chromatography ◽  
Serine Proteinases ◽  
Guanidinium Chloride ◽  
Nasal Cartilage ◽  
Thiol Proteinases

Extracts from bovine nasal cartilage with 1 M-guanidinium chloride were fractionated by ultrafiltration. Gel chromatography of the low-molecular-weight material resolved three distinct fractions with inhibitory activity against (a) collagenases (22000 mol.wt.), (b) thiol proteinases cathepsin B and papain (13000 mol.wt.), and (c) trypsin and other serine proteinases (7000 mol.wt.).

Inhibition of the cathepsin B like proteinase by a low molecular weight cysteine-proteinase inhibitor from ascitic fluid and plasma α2 macroglobulin

1986 ◽  
Vol 64 (12) ◽  
pp. 1218-1225 ◽  
Author(s):  
Maurice Pagano ◽  
Daniel Keppler ◽  
Veronique Fumeron-Dalet ◽  
Robert Engler
Keyword(s):  
Molecular Weight ◽  
Ascitic Fluid ◽  
Cathepsin B ◽  
Proteinase Inhibitors ◽  
Cysteine Proteinase ◽  
Low Molecular Weight ◽  
Cysteine Proteinase Inhibitor ◽  
Cysteine Proteinase Inhibitors ◽  
Α2 Macroglobulin ◽  
Endopeptidase Activity

The cathepsin B like proteinase present in ascitic fluid of a patient with neoplasia has been purified and characterized after pepsin activation. From this fluid we have prepared the low molecular weight (LMW) cysteine-proteinase inhibitors. Three major inhibitor forms were found with isoelectric points of 7.4, 5.4, and 5.1, respectively. The interaction of the enzyme with the former inhibitor was studied because this inhibitor was the most abundant. The Ki value was found to be 4.3 × 10−8 M. Two molecules of this proteinase were bound by one molecule of plasma α2 macroglobulin (α2M). The LMW inhibitor was able to bind to the enzyme entrapped in α2M and reduced its endopeptidase activity on benzyloxycarbonyl-L-phenylalanyl-L-arginine-4-methyl-7-coumarylamide. These results may have a physiological significance in the regulation of the enzyme which, among other extracellular hydrolases, probably plays an important role in tumor invasion.

The Relation Between VIIIR:AG and VIII:C Studied with Two Antisera

1979 ◽  
Author(s):  
H. P. Muller ◽  
N. H. van Tilburg ◽  
R. M. Bertina ◽  
J. J. Veltkamp
Keyword(s):  
Molecular Weight ◽  
High Salt ◽  
Low Molecular Weight ◽  
Gel Chromatography ◽  
Specific Antibodies ◽  
Specific Effects ◽  
Normal Plasma ◽  
Coagulant Activity ◽  
Sterical Hindrance ◽  
Inhibitory Antibodies

FVIII was separated into low molecular weight FVIII (LMW FVIII) and high molecular weight FVIII (HMW FVIII) by gel chromatography in the presence of high salt concentration or by high salt elution of LMW FVIII from FVIII bound to anti HMW FVII-Sepharose. Specific antibodies were raised in rabbits against HMW FVIII and LMW FVIII. After removal of the contaminating anti HMW activities the rabbit anti LMW FVIII was still able to neutralize the FVIII coagulant activity of normal plasma and of IMW FVIII with canparable efficiency and it had no effect on the VIIIR:WF of FVIII in normal plasma or in HMW FVIII. Anti LMW FVIII does not bind to HMW FVIII and does not precipitate FVIII as tested by counter immunoelectrophoresis. Rabbit anti HMW FVIII precipitates FVIII in normal plasma, inhibits VIIIR:WF activity, while it has no effect on the FVIII coagulant activity of LMW FVIII. The coagulant activity of FVIII in normal plasma is slightly inhibited by anti HMW FVIII presumably by non-specific effects (sterical hindrance). It is concluded that inhibitory antibodies against VIII:C raised in rabbits recognize antigenic structures only present on LMW FVIII. Antibodies against HMW FVIII raised in rabbits appears to recognize structures only present on HMW FVIII.

scholarly journals Novel Role for Albumin in Innate Immunity: Serum Albumin Inhibits the Growth of Blastomyces dermatitidis Yeast Form In Vitro

2003 ◽  
Vol 71 (11) ◽  
pp. 6648-6652 ◽  
Author(s):  
Steven Giles ◽  
Charles Czuprynski
Keyword(s):  
Molecular Weight ◽  
Inhibitory Activity ◽  
Mammalian Species ◽  
Blastomyces Dermatitidis ◽  
Low Molecular Weight ◽  
Rat Serum ◽  
Yeast Form ◽  
Domain Iii

ABSTRACT In this study we found that serum inhibitory activity against Blastomyces dermatitidis was principally mediated by albumin. This was confirmed in experiments using albumin from several mammalian species. Analbuminemic rat serum did not inhibit B. dermatitidis growth in vivo; however, the addition of albumin restored inhibitory activity. Inhibitory activity does not require albumin domain III and appears to involve binding of a low-molecular-weight yeast-derived growth factor.

Hepatic Metallothionein in Rainbow Trout (Salmo gairdneri) as an Indicator of Metal Pollution in the Campbell River System

1982 ◽  
Vol 39 (12) ◽  
pp. 1596-1601 ◽  
Author(s):  
M. Roch ◽  
J. A. McCarter ◽  
A. T. Matheson ◽  
M. J. R. Clark ◽  
R. W. Olafson
Keyword(s):  
Molecular Weight ◽  
Rainbow Trout ◽  
Metal Pollution ◽  
Quantitative Measure ◽  
Salmo Gairdneri ◽  
Differential Pulse Polarography ◽  
Low Molecular Weight ◽  
Gel Chromatography ◽  
Hepatic Metallothionein ◽  
Molecular Weight Fractions

Hepatic metallothionein was measured in livers of freshly killed rainbow trout (Salmo gairdneri) using differential pulse polarography. The fish were caught in metal-contaminated lakes of the Campbell River watershed and in a nearby control lake. The livers were analyzed for zinc, copper, and cadmium using atomic absorption spectrophotometry. High and low molecular weight protein fractions were separated by gel chromatography from liver cytosols and analyzed for metals. A downward trend from the most contaminated lake to the least was found in levels of zinc in the water, of cadmium and copper in high molecular weight fractions, and of copper in low molecular weight fractions and metallothionein. The concentration of metallothionein is a useful quantitative measure of the degree of exposure of fish to heavy metals.Key words: metallothionein, rainbow trout, Salmo gairdneri; heavy metal pollution, sublethal exposures, mine wastes

scholarly journals Detection, purification and characterization of a human cancer-associated galactosyltransferase acceptor

1979 ◽  
Vol 178 (2) ◽  
pp. 279-287 ◽  
Author(s):  
D K Podolsky ◽  
M M Weiser
Keyword(s):  
Molecular Weight ◽  
Human Cancer ◽  
Deae Cellulose ◽  
Structural Data ◽  
Low Molecular Weight ◽  
Gel Chromatography ◽  
Purification And Characterization ◽  
Peptide Moiety ◽  
Cellulose Column

A low-molecular-weight acceptor of galactosyltransferase activity was detected in sera and effusions of patients with extensive maligant disease. This substance was purified to homogeneity from both human serum and effusion by using sequential charcoal/Celite and DEAE-cellulose column chromatography. The purified acceptor was shown to act as substrate for both purified normal and cancer-associated human galactosyltransferase (EC 2.4.1.22) isoenzymes, but had a higher affinity for the cancer-associated isoenzyme (Km = 20 microM) than for the normal isoenzyme (Km = 500 microM). The substrate was found to be a glycopeptide with mol.wt. approx. 3600 determined by polyacrylamide-gel chromatography. Carbohyydate analysis demonstrated only the presence of glucosamine and mannose. Amino acid analysis revealed that the peptide moiety consisted of eight different amino acids, including two residues of asparagine and one residue of serine, but no threonine. These structural data suggest that the acceptor is a fraction of an asparagine-glucosamine type of glycoprotein.

scholarly journals Structure Analysis and Anti-Tumor and Anti-Angiogenic Activities of Sulfated Galactofucan Extracted from Sargassum thunbergii

Marine Drugs ◽  
2019 ◽  
Vol 17 (1) ◽  
pp. 52 ◽  
Author(s):  
Weihua Jin ◽  
Wanli Wu ◽  
Hong Tang ◽  
Bin Wei ◽  
Hong Wang ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Molecular Weight ◽  
High Molecular Weight ◽  
Structure Analysis ◽  
Nmr Spectra ◽  
Low Molecular Weight ◽  
Gel Chromatography ◽  
Sargassum Thunbergii ◽  
Sulfation Pattern ◽  
Fucose Content

Sulfated galactofucan (ST-2) was obtained from Sargassum thunbergii. It was then desulfated to obtain ST-2-DS, and autohydrolyzed and precipitated by ethanol to obtain the supernatant (ST-2-S) and precipitate (ST-2-C). ST-2-C was further fractionated by gel chromatography into two fractions, ST-2-H (high molecular weight) and ST-2-L (low molecular weight). Mass spectrometry (MS) of ST-2-DS was performed to elucidate the backbone of ST-2. It was shown that ST-2-DS contained a backbone of alternating galactopyranose residues (Gal)n (n ≤ 3) and fucopyranose residues (Fuc)n. In addition, ST-2-S was also determined by MS to elucidate the branches of ST-2. It was suggested that sulfated fuco-oligomers might be the branches of ST-2. Compared to the NMR spectra of ST-2-H, the spectra of ST-2-L was more recognizable. It was shown that ST-2-L contain a backbone of (Gal)n and (Fuc)n, sulfated mainly at C4 of Fuc, and interspersed with galactose (the linkages were likely to be 1→2 and 1→6). Therefore, ST-2 might contain a backbone of (Gal)n (n ≤ 3) and (Fuc)n. The sulfation pattern was mainly at C4 of fucopyranose and partially at C4 of galactopyranose, and the branches were mainly sulfated fuco-oligomers. Finally, the anti-tumor and anti-angiogenic activities of ST-2 and its derivates were determined. It was shown that the low molecular-weight sulfated galactofucan, with higher fucose content, had better anti-angiogenic and anti-tumor activities.

Detection of low molecular weight cysteine proteinase inhibitors by time-resolved fluoroimmunoassay

1986 ◽  
Vol 86 (2) ◽  
pp. 243-247 ◽  
Author(s):  
I. Joronen ◽  
V.K. Hopsu-Havu ◽  
M. Manninen ◽  
A. Rinne ◽  
M. Järvinen ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Proteinase Inhibitors ◽  
Cysteine Proteinase ◽  
Low Molecular Weight ◽  
Time Resolved ◽  
Cysteine Proteinase Inhibitors

scholarly journals Purification and structural characterization of a cartilage matrix protein

1981 ◽  
Vol 197 (2) ◽  
pp. 367-375 ◽  
Author(s):  
M Paulsson ◽  
D Heinegård
Keyword(s):  
Molecular Weight ◽  
Matrix Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Cartilage Matrix ◽  
Sedimentation Equilibrium ◽  
Intact Protein ◽  
Gel Chromatography ◽  
Guanidinium Chloride ◽  
Cscl Density Gradient

The cartilage matrix protein is a major non-collagenous protein in bovine cartilage. It was purified from a 5 M-guanidinium chloride extract of bovine tracheal cartilage by sequential CsCl-density-gradient centrifugation, gel chromatography in guanidinium chloride and differential precipitation. The molecular weight of the intact protein is 148 000, determined by sedimentation-equilibrium centrifugation. It was dissociated to three subunits of molecular weight 52 000 by reduction of disulphide bonds. The cartilage matrix protein was insoluble in low-salt solutions and behaved abnormally on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. The content of cysteine was high, whereas the contents of aromatic amino acids were low. The carbohydrate content was 3.9% (w/w). Glycopeptides obtained after papain digestion were heterogenous on gel chromatography. Asparagine/aspartic acid was enriched in the purified glycopeptides, indicating the presence of N-glycosidic linkages to protein.

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