Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.1 (chymotrypsin)
 10,938 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Lysosomal fraction was isolated from rat liver by density gradient centrifugation after pervious loading of lysosomes in vivo with Triton WR-1339. Tritosome preparations were incubated at 37 degrees C and pH 5 for 24 hr with purified human ceruloplasmin or haptoglobin. After this period approximately 20% of total alpha amino nitrogen was released from ceruloplasmin and over 40% from haptoglobin. This was accompanied by loss of peroxidase activity of haptoglobin (in complex with haemoglobin), while enzymatic activity of ceruloplasmin remained unaltered. Removal of sialic acid by neuraminidase had no effect on digestion of ceruloplasmin by rat liver tritosomes. Both glycoproteins were resistant to horse leucocyte proteinases and pancreatic eleastase but were easily inactivated by trypsin and chymotrypsin.
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PMID:Degradation and inactivation of ceruloplasmin and haptoglobin by rat liver lysosomes and some other proteinases. 65 34

Characterization of the cyanogen bromide (CNBr) fragments of the beta chain of human haptoglobin revealed five major fragments resulting from cleavage of four methionyl residues. The fragments were isolated by gel filtration in guanidine-HCl on Sepharose 6B and Bio-Gel P10 and P60. Compositional analyses of the five cyanogen bromide fragments accounted for 248-253 amino acid residues in agreement with the number of residues determined for the intact beta chain. Most of the carbohydrate was attached to CNBr II. Automated amino-terminal sequence analysis and carboxyl-terminal hydrolysis with carboxypeptidase of the haptoglobin beta chain and cyanogen bromide fragments identified 139 residues, or about 55% of the beta-chain molecule. The placement of the fragments within the beta-chain molecule was established by sequence analysis of whole beta chain and a plasmin cleavage fragment. The position of CNBr V was confirmed by the absence of homoserine or homoserine lactone. Cyanogen bromide reaction of intact haptoglobin 1-1 resulted in the isolation of a beta-chain fragment, CNBr III, covalently attached to the intact alpha1 chain by a single disulfide bond. The beta chain was shown to have primary structural similarities to the chymotrypsin family of serin eproteases. Partial sequence analysis of CNBr V established the region which is comparable to the serine-195 active-site region: /Asp-Thr-Cys-Tyr-Gly-Asp-Ala-Gly-Ser-Ala-Phe/ (residues 189-199, chymotrypsinogen A numbering). The active-site serine-195 is replaced by alanine; however, the specificity residue of the trypsin-like enzymes, Asp-189, is preserved. Several minor cyanogen bromide cleavage products were also identified in yields of up to 15%. These minor cleavage products give evidence that tryptophanyl residues in proteins, or glycoproteins, are also susceptible to cyanogen bromide cleavage.
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PMID:Characterization of the cyanogen bromide fragments of the beta chain of human haptoglobin. 99 9

The influence of diclofenac, given by continuous i.v. infusion starting preoperatively, on postoperative pain and inflammation was assessed in a double-blind, randomized, placebo-controlled study in 40 patients scheduled for major orthopedic surgery. Starting 30 min before induction the patients received either diclofenac (0.35 mg.kg-1 bolus followed by a constant-rate infusion of 90 micrograms.min-1) or placebo for 24 h. The pain intensity (VAS) and the amount of rescue narcotic (piritramide on demand) were significantly lower in the diclofenac group from 4 and 6 h postsurgery, respectively, till end of infusion. Acute phase proteins used as inflammation markers (C-reactive protein, alpha 1-chymotrypsin, alpha 1-acid glycoprotein, haptoglobin and coeruloplasmin) showed similar variations in both groups for 24 h. The diclofenac treatment had no influence on hematological and coagulation profiles, nor on muscle and liver enzymes in comparison with placebo. Both patients and observer rated the diclofenac treatment as significantly superior to the placebo treatment.
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PMID:Prophylactic diclofenac infusions in major orthopedic surgery: effects on analgesia and acute phase proteins. 137 1

A human hepatoma cell line, associated with thorotrast exposure, from an hepatitis B marker-negative patient was established as a permanent cell line (Mz-Hep-1) in tissue culture. Histology of the primary tumor, as well as phase contrast, transmission and scanning electron microscopy of the cultured cells showed typical characteristics of liver cells. Mz-Hep-1 cells secreted complement components (C2, C3, C4), carcinoembryonic antigen, lactate dehydrogenase, chymotrypsin, haptoglobin and retinol-binding protein and expressed HLA-, transferrin-, blood group B-related determinants and complement component C5 and carcinoembryonic antigen on their cell surface. Mz-Hep-1 cells represent the first human hepatoma cell line, which is strongly associated with a carcinogen.
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PMID:Hepatocellular carcinoma after thorotrast exposure: establishment of a new cell line (Mz-Hep-1). 241 35

The antiproteinase activities against trypsin, chymotrypsin, elastase, papain and rat leucocyte proteinases were determined in plasma from control and Morris hepatoma-bearing rats. Bovine trypsin and chymotrypsin were similarly inhibited by the two types of plasma whereas porcine pancreatic elastase, papain and rat leucocyte neutral proteinases were more efficiently inhibited by plasma from tumour-bearing rats. The increased plasma concentrations of some proteinase inhibitors, as determined by rocket immunoelectrophoresis, are suggested to be responsible for the observed differences in inhibition. The highest increases in plasma of tumour-bearing rats were observed for alpha 2-macroglobulin and alpha 1-acute-phase globulin. The synthesis and secretion of six proteinase inhibitors: antithrombin III, alpha 1-proteinase inhibitor, alpha 1-macroglobulin, alpha 2-macroglobulin, alpha 1-acute-phase globulin and haptoglobin, as well as albumin, were measured in tissue slices from rat liver and Morris hepatoma after incubation with [14C]leucine. Local inflammation inflicted upon the tumour-bearing rats increased formation of acute-phase proteins in liver slices but not in hepatoma slices.
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PMID:Plasma proteinase inhibitors in Morris hepatoma-bearing rats: changes in the blood level and synthesis in tissue slices. 407 27

An inflammatory reaction protein is a protein whose rate of synthesis is greater than its rate of catabolism in the presence of an inflammatory process. This is reflected by an increase in its plasma concentration. In man, orosomucoid, alpha-1 antitrypsin, alpha-1 anti-chymotrypsin, haptoglobin, ceruloplasmin, fibrinogen and C reactive protein (CRP), all conform to this definition. The authors present the principal physicochemical properties of the proteins. However, none of these proteins, on its own, constitutes an ideal marker of inflammation. The authors also propose the use of an inflammatory miniprofile consisting of "CRP, orosomucoid and haptoglobin" to detect, quantify and follow an inflammatory reaction. The authors stress the importance of using a rapid assay technique like immunonephelemetry , which is essential for the clinical usefulness of these proteins. Finally, they discuss the process of synthesis and the biological role of these proteins.
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PMID:[Proteins of the inflammatory reaction. Definition, physiology and methods for determination]. 620 41

Selective proteolysis has been used to delineate the hemoglobin-binding site on haptoglobin heavy chain. Haptoglobin was cleaved specifically by plasmin, trypsin, chymotrypsin, staphylococcal protease, and thermolysin. Haptoglobin-hemoglobin complex was treated with these enzymes to determine which sites were protected from cleavage by the hemoglobin. The modified haptoglobins were tested for changes in their hemoglobin and hemoglobin alpha chain-binding properties. The sites of proteolytic cleavage were identified from the newly generated NH2 termini by automated Edman degradation amino acid-sequencing techniques. The results suggest that residues 128 through 131, 136 and 137, as well as 9 and 10 of the heavy chain may be involved in the binding of hemoglobin. On the other hand, residues 159 and 160, which lie in the 17-residue additional loop that is unique to haptoglobin among its homologous serine protease family, and residues 73 and 74, which lie close to the carbohydrate-binding residues, appear to be remote from the hemoglobin-binding site.
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PMID:Hemoglobin-binding site on haptoglobin probed by selective proteolysis. 621 62

Parenteral nutrition (PN) is commonly used in the management of inflammatory bowel disease. Previously we reported about the serum protein levels in Crohn's disease before and after treatment with PN; in that study we found an increase of some indicators of nutritional status and a decrease of some acute phase reactants after treatment. We have now completed the trial determining the concentration of 19 serum proteins in 25 patients with Crohn's disease before and after treatment with PN and 8 wk thereafter. The concentration of albumin, retinol-binding protein, prealbumin, and transferrin were found to rise in parallel with the body weight during PN, whereas 8 wk after treatment only albumin and transferrin showed a further significant rise. alpha-1-Glycoprotein, alpha-2-chymotrypsin, alpha-1-antitrypsin, CRP, and haptoglobin decreased during and 8 wk after PN, alpha-1-glycoprotein, alpha-2-chymotrypsin, and alpha-1-antitrypsin showed a positive correlation to the Crohn's Disease Activity Index. The serum IgM-levels were found to be significantly increased during and after PN with a negative correlation to the Crohn's Disease Activity Index. Our data indicate that PN not only improves nutritional status in the active phase of Crohn's disease during therapy but reduces the grade of inflammatory activity during and even after treatment with PN.
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PMID:Influence of parenteral nutrition on serum levels of proteins in patients with Crohn's disease. 641 11

The concentration of 19 serum proteins was determined by radial immunodiffusion in 23 patients with Crohn's disease before and after treatment with parenteral nutrition. The results were related to body weight and Crohn's Disease Activity Index. An increased serum concentration of retinol-binding protein, prealbumin, and transferrin paralleled an increase of body weight. Alpha-1-glycoprotein, alpha-2-chymotrypsin, alpha-1-antitrypsin, C-reactive protein, and haptoglobin decreased during parenteral nutrition and showed a positive correlation to the Crohn's Disease Activity Index. The determination of certain proteins is clinically useful, since their serum concentration reflects the influence of parenteral nutrition on nutritional status and disease activity. Measurement of these proteins provides a useful guide to the management of patients with Crohn's disease treated with parenteral nutrition.
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PMID:[Effect of parenteral nutrition on serum proteins in patients with Crohn disease]. 680 21

A model has been constructed for haptoglobin heavy chain by using the known sequence homology to the mammalian serine proteases. The three-dimensional structures for three serine proteases, chymotrypsin, trypsin, and elastase, were compared and the structural features that are conserved in all three were extracted. The haptoglobin heavy chain sequence was aligned to the sequences of the three serine proteases by maximizing sequence homology in the regions of conserved structure. The resulting alignment shows that haptoglobin heavy chain must be very closely homologous to these proteases in structure as well as in sequence. Coordinates were derived for the heavy chain by using the homologous structures. The problems associated with these coordinates are outlined and methods for solving them are indicated. The features of the haptoglobin heavy chain structure are described. Implications of the structure for the very strong interaction between this subunit and hemoglobin are discussed.
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PMID:Model for haptoglobin heavy chain based upon structural homology. 693 26


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