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

The bovine pancreatic inhibitor of trypsin (trasylol, Bayer) (T) and the soy bean trypsin inhibitor (SBI) were coupled with peroxidase (P). With each one of these coupling products (T and P and SBI and P) the cell distribution of proteolytic enzymes (PE) of ascitic cells of L5178Y murine lymphoma, was localized. The reactions were developed by means of Karnowsky's reaction with diaminobenzidine and H2O2. The preparations were observed under light and electronic microscopy. It was found that L5178Y cells contain intracellular PE in granules measuring 0.1 to 0.8 min diameter, and superficial PE that form a continuous layer of 80 to 120 nm over the cell surface. Superficial PE were not identified in 20 per cent of L5178Y cells, while in every case intracellular granules were found. Both the macrophages and the polimorphonuclear cells present in the ascitic fluid contained intracellular PE granules measuring 0.05 to 0.4 micron in diameter, and did not contain superficial PE.
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PMID:Proteolytic enzymes marking of malignant lymphoblasts, study of the L5178Y murine lymphoma. 63 54

Plasminogen activator activity was determined in human follicular fluids (FFs) obtained during in vitro fertilization procedures. The fibrinolytic activity of plasminogen activator was significantly higher in fluids from follicles that contained oocytes that were later found to fertilize in vitro (group F) as compared with fluids from follicles that contained oocytes that failed to fertilize (NF). To assess whether this difference in overt plasminogen activator activity reflects differences in conversion of an inactive, latent plasminogen activator to the active enzyme, the ability of exogenous trypsin to enhance plasminogen activation was measured. The plasminogen-dependent hydrolysis of the chromogenic substrate S-2444 in presence of trasylol (Bayer, Leverkusen, Germany) was taken as a measure of plasminogen activator activity in these experiments. No activity was found in untreated FFs, while exposure to trypsin resulted in emergence of marked plasminogen activator activity. In addition, FFs exhibited trasylol-sensitive chromogenic activity indicative of serine-protease activity. Both the plasminogen activator and serine-protease levels after tryptic activation were significantly higher in NF than in F samples. Thus, while F samples have most of their plasminogen activator in an active form, NF samples have most of their plasminogen activator in a latent, trypsin-activatable form. Follicular fluids also contain inhibitory activities toward plasmin and trypsin. The inhibition of these enzymes correlates positively with the latency of plasminogen activator. These results suggest a direct relationship between the ability of oocytes to fertilize and the overt to latent plasminogen activator activity ratios in the FFs.
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PMID:Human follicular fluid protease and antiprotease activities: a suggested correlation with ability of oocytes to undergo in vitro fertilization. 252 54

Examination of the peritoneal exudates of 12 patients with acute pancreatitis revealed high activities of pancreatic lipase and amylase. The immunologic levels of the plasma-derived inhibitors alpha 1-antitrypsin, antithrombin III and alpha 2-macroglobulin in the peritoneal exudates were not markedly different from those of the plasma. However, the inhibitory capacity of alpha 2-macroglobulin, the main inhibitor of human pancreatic trypsin in the exudate, was almost completely depleted when measured by an enzymatic method. Furthermore, spontaneous fibrinolysis occurred in 6 out of 13 exudates applied to plasminogen-free fibrin plates, indicating the presence of free proteinase. This fibrinolytic activity might be inhibited by exogenous alpha 2-macroglobulin or aprotinin (Trasylol, Bayer AG).
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PMID:Proteinases and inhibitors in plasma and peritoneal exudate in acute pancreatitis. 608 67

It has been reported that polyclonal B cell stimulation results in formation of autoantibodies and immune complexes. We have previously reported that a polyclonal B cell activator (PBA) associated with alpha 2-macroglobulin (alpha 2M) is present in the serum of patients with rheumatoid arthritis and related diseases. Here we studied the possibility that patient alpha 2M (Pt-alpha 2M) carries a trypsin-like protease responsible for the PBA activity. This activity was determined by the Ig-turnover assay developed in our laboratories. The small molecular weight protease inhibitors, aprotinin (Trasylol, Bayer) and phenylmethylsulfonylfluoride (PMSF), and the large molecular weight soybean trypsin inhibitor (SBTI) were used. These inhibitors did not affect the PBA activity of dextran sulfate of LPS. However, as expected, trypsin had a PBA-activity which was blocked by all of the above mentioned inhibitors. A trypsin-normal alpha 2M complex (Tr-N alpha 2M) and PBA activity which was inhibited by PMSF or aprotinin but not by SBTI. The PBA associated with Pt-alpha 2M was also inhibited by PMSF or aprotinin but not by SBTI. Moreover, the Tr-N alpha 2M complex and the Pt-alpha 2M, but not that from normal donors, had esterase activity for p-toluenesulfonyl-L-argininemethyl ester. These data suggest a similarity between the Pt-alpha 2M and Tr-N alpha 2M complex. Thus, we concluded that the esterolytic activity is sufficient for PBA activity, that Pt-alpha 2M has esterolytic activity and that this PBA activity can be blocked by small molecular weight protease inhibitors.
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PMID:The effect of protease inhibitors on the polyclonal B cell activator from the serum of patients with rheumatoid arthritis. 617 49

Ascaris trypsin inhibitors 1, 2, and 3 have arginine at their reactive P1 site. This corrects an earlier report that lysine is the reactive P1 site residue in Ascaris trypsin inhibitor 1 (Peanasky et al., 1974, Bayer Symposium V: Proteinase Inhibitors, pp. 649-666). The present work illustrates that the residue modification method of Fritz et al. (1969, Z. Physiol. Chem., 350, 933-944) may not be reliably interpreted when trypsin inhibitors have an unusually high lysine content (greater than 12% of the molecular weight of the inhibitor). Thus the following procedure is recommended: treat the inhibitor with maleic anhydride first and second with butanedione reagent; then remove the maleyl groups in an acid environment and determine the activity of the inhibitor. Immunoperoxidase staining shows that antibody to Ascaris trypsin inhibitor 1 binds to body wall muscle, intestine, eggs and sperm in cross-sections of Ascaris. Antibody to TLCK-porcine trypsin binds to the same tissues and at the same sites as the antibody to Ascaris trypsin inhibitor 1. This is the first demonstration that a protein that originated in the host has been found in the parasite, Ascaris. Analyses of homogenates and of extracts of separated tissues always show an excess of free trypsin inhibitor and no evidence of active trypsin. The host protein is present inside the parasite, probably as the trypsin-inhibitor complex.
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PMID:Trypsin inhibitors from Ascaris: the reactive P1 site of the inhibitors (a correction) and location of the inhibitors and host trypsin in cross-sections of Ascaris. 640 61

The positions, with respect to the plasma membrane, of lysine 905, contained in the peptide QRKIVE, and of lysine 1012, contained in the carboxy-terminal peptide, RPGGWVEKETYY, of ovine Na+/K(+)-transporting ATPase have been reported to be cytoplasmic and extracytoplasmic, respectively [Bayer, R. (1990) Biochemistry 29, 2551-2256]. These results from our laboratory have been reexamined using an extension of the same procedure. Sealed right-side-out vesicles were modified with pyridoxal phosphate and sodium [3H]borohydride in the presence and absence of saponin or cholate. The modified alpha polypeptide was isolated and digested with the proteinase from Staphylococcus aureus strain V8 or trypsin to produce one or the other of these two peptides. These digests were passed over immunoadsorbents, identical to those used by Bayer, directed against pyroglutamylRXIVE or -ETYY. Unlike in the earlier studies, however, in the present studies the modified, radioactive peptides bound and eluted from the immunoadsorbents were submitted to HPLC, and their respective mobilities were compared to those of the synthetic peptides that had also been modified with pyridoxal phosphate. In this manner, the correct, modified peptide could be positively identified, and its specific radioactivity could be estimated. When cholate was added to sealed vesicles, prior to modification, there was at least a 3-fold increase in the incorporation of radioactivity into lysine 1012, consistent with a cytoplasmic location for this residue.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:The carboxy terminus of sodium and potassium ion transporting ATPase is located on the cytoplasmic surface of the membrane. 838 80

The Bayer Immuno 1 PSA Assay measures total PSA in human serum and demonstrates excellent performance with an interassay CV < or = 3.4% and a biological detection limit of 0.03 microgram/L. No significant interference from common hormonal and chemotherapeutic drugs, kallikrein, prostatic acid phosphatase, and trypsin, or elevated levels of total bilirubin, hemoglobin, triglycerides, and IgG was observed. The 95th percentile values for healthy individuals increased with age from 3.0 micrograms/L for males 50-59 years and 3.3 micrograms/L for males 60-69 years, to 4.6 micrograms/L for males > or = 70 years. Clinical studies with retrospective samples demonstrated correspondence between serial measurements of PSA and clinical outcome for 98% of 159 prostate cancer patients. Clinical sensitivity for patients with clinical evidence of disease, untreated at the time of specimen draw, increased with increasing stage from 77.5-100%. Specificity of 60-70% for BPH and other benign urogenital diseases was consistent with previous findings. Bayer Immuno 1 PSA Assay values for 2131 specimens from healthy subjects and patients with prostate cancer, BPH, and other malignant and nonmalignant diseases correlated well with the Abbott IMx PSA Assay over the range 0.0-6,238 micrograms/L (Y = 1.10 x + 0.02). The Bayer Immuno 1 PSA Assay provides automated ultrasensitive, precise, and equimolar measurement of total PSA in human serum.
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PMID:Bayer Immuno 1 PSA Assay: an automated, ultrasensitive method to quantitate total PSA in serum. 948 72