Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.4 (trypsin)
 42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A total of 31 strains of oral streptococci representing Streptococcus mutans, Streptococcus sanguis, Streptococcus mitior, Streptococcus salivarius, and Streptococcus milleri were tested for possible binding of human immunoglobulins G, G1, G2, G3, G4, A1, A2, M1, and M2 and haptoglobin, hemoglobin, fibrinogen, and aggregated beta 2-microglobulin. Radiolabeled beta 2-microglobulin in aggregated form showed affinity for 20 of the 31 strains tested. Binding activity for the protein was found in strains belonging to all five species. The bacterial receptor was resistant to trypsin. Monomeric, unlabeled beta 2-microglobulin did not interfere with the binding of the aggregated form. Of the other proteins tested, only the immunoglobulin A1 protein showed positive binding, and that was only with a single strain of S. milleri. beta 2-Microglobulin is present on all nucleated cell membranes in vivo. The reaction between aggregated beta 2-microglobulin and oral streptococci is a new type of human-bacterium interaction which should be considered in studies of bacterial adherence.
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PMID:Interactions between human serum proteins and oral streptococci reveal occurrence of receptors for aggregated beta 2-microglobulin. 9 15

Parallel determinations were made, of 10 individual serum proteins and of proteins in the bronchial secretion obtained by aspiration from 8 subjects that did not show manifest bronchopulmonary disease. By application of the formula suggested by Deuschl and Johansson it was found that 37 percent of IgG, 84,5 percent of IgA, 48,9 percent of transferrins, 15,2 percent of alpha-1-anti-trypsin and 11,3 percent of ceruloplasmin present in the bronchial secretion are synthetised in the bronchial mucosa itself, while the rest occur as a result of diffusion from the blood. Acid alpha-1-glycoprotein and haptoglobin from the bronchial secretion originate in the blood. IgM was evidenced in the bronchial aspirate in only 3 subjects, and alpha-2 macroglobulin was not found in any of the subjects.
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PMID:[Studies of the proteins in normal bronchial secretion]. 22 41

The cloning potential of PHA-treated T cells is significantly enhanced when lymphocyte culture fluid (LCF) from mitogen-treated lymphocytes is added to the soft agar culture system. The mitogens seem to stimulate the release of a lymphocyte colony enhancing factor (LCEF) into the culture medium. A study of the physico-chemical properties of the LCEF revealed that it is a nondialyzable, heat-labile molecule which migrates in the haptoglobin (2--2) post-transferrin region in acrylamide electrophoresis. It is stable to RNase and DNase but labile to papain and trypsin. The LCEF was partially purified from the crude LCF using a sequence of techniques--ammonium sulphate precipitation, DEAE-cellulose and Bio-Gel P-150 chromatography and disc electrophoresis. The mol. wt of the purified LCEF, determined from gel filtration chromatography, was 90,000--110,000.
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PMID:Partial purification and characterization of the human lymphocyte colony enhancing factor (LCEF). 30 93

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

In women employed in an industrial plant in direct contact with epoxide resins and their hardeners, the following biochemical parameters were determined in blood: total protein, seromucoid, haptoglobin, hemoglobin variants, methemoglobin, alpha1-inhibitor of trypsin, lactate dehydrogenase, aspartate and alanine aminotransferases, alkaline and acid phosphatase, gamma-glutamyl transpeptidase, leucylaminopeptidase, and alanine aminopeptidase. Depending on duration of work, Hb A2 fraction and lactate dehydrogenase increased significantly, and aspartate aminotransferase, acid and alkaline phosphatase activities decreased. In pregnant women, leucylaminopeptidase activity and isozyme of placental alkaline phosphatase were decreased.
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PMID:Evaluation of the influence of epoxide resins and their hardeners on the female body. II. Biochemical studies. 101 94

Thirty-three patients with esophageal cancer were studied to assess the relationship between nutritional state and the acute phase protein responses. Blood samples taken preoperatively and days 1, 4, 7 and 14 after operation were analyzed for C-reactive protein, fibrinogen, alpha 1-antitrypsin, alpha 1-acid glycoprotein and haptoglobin. Significant Spearman's coefficients were found between percent of ideal body weight (IBW) and alpha 1-acid glycoprotein (r = -0.42), between prealbumin and alpha 1-anti-trypsin (r = -0.55), and between retinol-binding protein and alpha 1-antitrypsin (r = -0.51). Postoperatively, the levels of C-reactive protein, fibrinogen, alpha 1-anti-trypsin and alpha 1-acid glycoprotein were significantly lower in the poorly nourished group than in the other groups. The changes of acute phase proteins in the immediate postoperative period were affected by the preoperative nutritional state, and were less marked in the poorly nourished patients. Between two groups of patients in whom lymph node dissection was carried out in 2 or 3 areas, no significant differences were observed in the acute phase protein responses postoperatively. The measurement of acute phase proteins is very important in assessing the body defense capacity of the patient, but it should be noted that the changes may be affected by several factors including malnutrition.
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PMID:[Postoperative changes in acute phase protein in patients with esophageal cancer]. 138 Jun 33

This paper describes the development of a murine bank of monoclonal antibodies against Bordetella pertussis toxin, filamentous hemagglutinin (FHA), pili, lipopolysaccharide (LPS), or outer membrane proteins (OMPs). Subunits S1, S2, S3 of pertussis toxin (PT) bound immunoglobulins and glycoproteins such as fetuin and haptoglobin in an unspecific manner. The specificity of monoclonal antibodies towards subunits S1, S2, S3 or S4 of PT could be demonstrated by using purified immunoglobulins or their Fab2 fragments. A set of FHA-specific monoclonal antibodies could be differentiated on the basis of their binding to the various breakdown products present in FHA preparations. Pili-specific monoclonal antibodies reacted with either native pili or denatured pilin, and both demonstrated serotype specificity. Monoclonal antibodies to Bordetella pertussis OMPs were directed to either the virulent phase-regulated trypsin-sensitive, detergent-extractable OMPs 92 kDa, 32 kDa, and 30 kDa or the non-virulent phase-expressed, not-trypsin sensitive OMPs 38 kDa, 33kDa, and 18 kDa.
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PMID:Description of a hybridoma bank towards Bordetella pertussis toxin and surface antigens. 198

All 25 cultures of Actinomyces pyogenes tested in the present study bound 125I-labelled human alpha 2-macroglobulin with a mean binding of 65.6%. Thirteen cultures also bound 125I-labelled human haptoglobin with a mean of 51.5%. None interacted with fibrinogen, fibronectin, immunoglobulin G, or albumin. Twenty-eight cultures representing other species of actinomycetaceae did not show any interaction with alpha 2-macroglobulin, haptoglobin, and other plasma proteins tested. The binding of alpha 2-macroglobulin and haptoglobin to A. pyogenes was saturable and could be completely inhibited by the respective unlabelled plasma proteins. The binding of alpha 2-macroglobulin could not be inhibited by unlabelled haptoglobin. On the other hand, alpha 2-macroglobulin blocked the binding of haptoglobin, possibly by steric hindrance. Treatment of the bacteria with trypsin reduced their binding activities for alpha 2-macroglobulin and haptoglobin indicating the protein nature of the binding sites. Exposure to heat (1 h, 80 degrees C) significantly diminished the binding activity for haptoglobin, but not that for alpha 2-macroglobulin. The binding of alpha 2-macroglobulin and haptoglobin could be an important feature in the classification of A. pyogenes among the members of actinomycetaceae.
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PMID:Binding of alpha 2-macroglobulin and haptoglobin to Actinomyces pyogenes. 241 71

Immunofluorescence staining in unfixed or fixed renal biopsy specimens were evaluated in nine patients with diabetic nephropathy in order to elucidate if immunofluorescence staining is applicable in fixed renal tissues in such patients. Renal biopsy specimens were embedded in gelatin or paraffin matrix. Renal biopsy specimens embedded in paraffin matrix were digested with 0.05% protease. Immunofluorescent studies of kidney tissues were performed by staining with FITC-labeled heavy chain specific anti-human IgG, IgA, IgM, acute phase reactant (APR) proteins such as alpha 1-anti-trypsin (alpha 1-AT), haptoglobin (Hpt) and beta-lipoprotein (beta-Lp) antisera, and then examined with a fluorescent microscope. Linear and nodular deposition of IgG, IgA, IgM, alpha 1-AT, Hpt, and beta-Lp were observed in the glomerular capillary walls of the renal specimens embedded in paraffin matrix. The staining patterns in specimens embedded in paraffin matrix was similar to that embedded in gelatin matrix. There was no significant difference in the intensity or distribution of IgG, IgM, alpha 1-AT, and beta-Lp deposition among the two different conditions of immunofluorescence in patients with diabetic nephropathy. It was suggested that immunofluorescence staining in renal biopsy specimens embedded in paraffin matrix after digestion with protease is useful for the evaluation of IgG, IgM, APR proteins, and beta-Lp in glomeruli from patients with diabetic nephropathy.
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PMID:Immunofluorescence staining in unfixed or fixed renal biopsy specimens from patients with diabetic nephropathy. 241 46


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