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Enzyme
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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)
The cationic proteins from neutrophil lysosomes have been shown to modulate phagocytic activity of granulocytes. The present study reports the effects of the cationic protein fractions on the generation of O2- by human PMNs during phagocytosis. Human PMNs were reacted with different phagocytic stimuli in the presence and absence of lysosomal cationic proteins and the amount of O2- generated was determined by superoxide dismutase inhibitable reduction of cytochrome c. Total cationic protein extract from neutrophil lysosomes enhanced O2- generated by PMNs during the phagocytosis of IgG-coated latex beads and opsonized zymosan particles. The analysis of the fractions of cationic proteins obtained from a Sephadex G-75 column showed that the O2- generation-enhancing activity was associated with the proteins eluted in fractions III and IV. A protein fraction mainly eluted in void volume inhibited the cytochrome c reduction by O2- formed during phagocytosis. This was due to the presence of superoxide dismutase-like activity since O2- generated by the xanthine-xanthine oxidase system was also inhibited by this fraction. The cationic protein fractions III and IV from the Sephadex G-75 column were further subfractionated. Although the O2(-)-enhancing activity was eluted in the same fractions as
chymotrypsin
activity, there was no quantitative correlation between the amount of O2- generation and
chymotrypsin
activity. Moreover, commercial
chymotrypsin
did not enhance O2- generation. Electrophoretic analysis of the isolated protein fractions suggests that O2- generation enhancing protein (SGEP) is different from
lysozyme
or
chymotrypsin
and probably represents previously undescribed protein.
...
PMID:Influence of neutrophil cationic proteins on generation of superoxide by human polymorphonuclear cells during phagocytosis. 303 79
A 68-year-old male with a myelodysplastic syndrome developed a bulla on his right thigh. A skin biopsy revealed a subepidermal cleavage containing fibrin and a mononuclear cell infiltrate exhibiting prominent erythrophagocytosis. Erythrophagocytosis by mononuclear cells was present, to a lesser extent, throughout the dermis and in the subcutis. Immunoperoxidase studies with anti-
lysozyme
and anti-alpha-l-
chymotrypsin
confirmed the histiocytic nature of the phagocytic cells. Only a few prior reports of cutaneous erythrophagocytosis exist in the literature. In contrast to the generally grave clinical manifestations of the patients described in previous publications documenting erythrophagocytosis, this patient lacked a concomitant hematologic deterioration or serious systemic illness.
...
PMID:Erythrophagocytosis in the skin: case report. 322 Sep 99
Histological material was studied in five unselected cases of intestinal large-cell non-Hodgkin's lymphoma, occurring in patients either with previously diagnosed coeliac disease, or with atrophic mucosa at the time of diagnosis. The morphological diagnosis in each case was centroblastic lymphoma: these tumours were composed of large cells with pale nuclei and prominent nucleoli. No phagocytosis was evident, but some cells showed considerable pleomorphism. Polykaryotic giant cells were infrequent. Immunohistochemical staining for
lysozyme
, alpha-1-anti-trypsin and alpha-1-anti-
chymotrypsin
failed to demonstrate any of these proteins in the tumour cells, although they were identified in accompanying reactive macrophages. There is thus no evidence for a histiocytic nature in these five cases. The tumours were immunoglobulin-negative. Again, polyclonal immunoglobulin could be demonstrated in reactive (plasma) cells in and near the tumour. The relevance of these immunological markers is discussed. We suggest that these tumours, and possibly some of those reported in a similar situation by other investigators, are in fact lymphocytic in origin. They are probably examples of centroblastic lymphoma, although T-cell lymphoma, rare in the gastrointestinal tract, cannot be ruled out by our immunohistological studies.
...
PMID:Large-cell intestinal lymphoma occurring in coeliac disease: morphological and immunohistochemical features. 348 59
Normal and metaplastic gastrointestinal mucosa obtained at surgical resection were studied by light microscopy, using the unlabelled antibody enzyme method for immunohistochemical staining of
lysozyme
, pancreatic endoproteases, and pancreatic secretory trypsin inhibitor (PSTI). Paneth cells in the mucosa of normal small intestine, gastric mucosa with intestinal metaplasia, and colonic metaplastic mucosa were found to contain anionic trypsin, cationic trypsin,
lysozyme
, and PSTI immunoreactivity, but not
chymotrypsin
and elastase immunoreactivity. Normal gastric and colonic mucosa and some goblet cells in the small intestine showed positive PSTI immunoreactivity but no endoprotease immunoreactivity. The presence of immunoreactive trypsin and immunoreactive PSTI in the Paneth cells, which are of secretory type, probably indicates an important extrapancreatic source of these proteins rather than a storage of endocytosed material.
...
PMID:Pancreatic endoproteases and pancreatic secretory trypsin inhibitor immunoreactivity in human Paneth cells. 352 12
The relation of lymphoma cells to gliomesenchymal stroma within nervous tissue was studied by peroxidase-antiperoxidase immunostaining of formalin-fixed and paraffin-embedded surgical specimens for fibronectin (FN), factor VIII-related antigen and glial fibrillary acidic protein in 17 malignant non-Hodgkin lymphomas of the brain. For comparison, 9 non-Hodgkin lymphomas, 6 Hodgkin lymphomas, and 19 plasmacytomas of the spinal or cranial epidural spaces were studied with the same methods. Lymphoma cells were consistently negative for all markers. All lymphomas of the brain showed conspicuous concentric perivascular circles of immunoreactivity for FN in parts infiltrating brain tissue. Such structures are considered to derive from splitting of basal laminae of preexisting brain vessels; they were not seen in tumors of the epidural space. Cells with conspicuous FN content were found in brain as well as in epidural lymphomas. A monohistiocytic origin of those cells was confirmed by presence of monohistiocytic markers
lysozyme
and alpha-1-anti-
chymotrypsin
. Thus, additional immunostaining for FN seems to be useful for detecting monohistiocytes/macrophages in brain tumors.
...
PMID:Development of stroma in malignant lymphomas of the brain compared with epidural lymphomas. An immunohistochemical study. 353 55
Acute megakaryocytic leukemia is a rare form of acute nonlymphocytic leukemia that occurs with increased frequency in patients with Down's syndrome. Herein, we report a child with Down's syndrome who presented with a large retroperitoneal mass due to acute megakaryocytic leukemia. Immunohistochemical stains of the tumor cells also demonstrated evidence of myeloid/monocytic differentiation, with positivity for alpha-1-antitrypsin, alpha-1-
chymotrypsin
, and
lysozyme
. The significance of this phenotypic heterogeneity is unclear and awaits further studies of similar cases.
...
PMID:Acute megakaryocytic leukemia with myeloid/monocytic differentiation. 367 84
Tryptophan pyrrolooxygenase from wheat germ was separated into three molecular forms by microgranular DEAE-cellulose using a stepwise or a linear gradient elution procedure. In the first case molecular forms A and B were eluted with 10 mM Tris/HCl buffer (pH 7.4) and molecular form C was eluted with 50 mM KCl in the same buffer. The same separation could also be achieved with a linear KCl gradient (0-100 mM) in 10 mM Tris/HCl buffer (pH 7.4). The three molecular forms of tryptophan pyrrolooxygenase oxidized L-, D-, DL-Trp as well as many Trp derivatives with formation of N-formylkynurenyl derivatives. They also efficiently oxidized Trp-Phe, Trp-Tyr, Trp-Ala, Ala-Trp, Trp-Gly, Gly-Trp, Trp-Leu, Leu-Trp, Pro-Trp and Val-Trp, although the dipeptides were oxidized at different rates by the three molecular forms. A number of tryptophyl-containing tetra-, penta-, octa-, nona- and decapeptides were also oxidized. The oligopeptides which were known to have a helical conformation were better substrates than the smaller oligopeptides which were devoid of the conformational factor. The three molecular forms of tryptophan pyrrolooxygenase oxidized the tryptophyl residues of
lysozyme
, pepsin,
chymotrypsin
, trypsin and bovine serum albumin. It was found that molecular form A oxidized the more exposed (or hydrophilic) Trp residues of the proteins, while molecular form C also oxidized the Trp residues of a more hydrophobic nature. The three molecular forms were inhibited by chelating agents (alpha, alpha'-dipyridyl, EDTA and omicron-phenanthroline), although they differed in their sensitivities to these agents. Their optimum temperatures and inactivation rates at 65 degrees C was also different.
...
PMID:Separation of tryptophan pyrrolooxygenase into three molecular forms. A study of their substrate specificities using tryptophyl-containing peptides and proteins. 369 18
Complexes of bilirubin with
chymotrypsin
,
lysozyme
and apomyoglobin in neutral aqueous solution are characterized by circular dichroism spectra in the visible region. These are analogous to previously investigated bilirubin-serum albumin complexes. Ferriprotoporphyrin IX displaces bilirubin from its apomyoglobin complex.
...
PMID:Complexes of bilirubin with proteins. 377 41
The amount of streptolysin S produced by resting streptococci was considerably increased after incubation of the washed bacteria with trypsin or pronase. Production of both cell-bound and free forms of the toxin was enhanced by the protease treatment. By addition of trypsin, streptolysin S yield was considerably increased in growing culture as well. Treatment with
lysozyme
was ineffective, and the toxin production was only slightly promoted by preincubation with hyaluronidase or
chymotrypsin
. In contrast, pretreatment with
chymotrypsin
caused increased production of an extracellular nuclease, whereas the yield of this enzyme was reduced after incubation of the cocci with pronase. Evidence was obtained indicating de novo synthesis of the exotoxin in the protease-treated bacteria.
...
PMID:Enhanced production of cell-bound and extracellular streptolysin S by hemolytic streptococci pretreated with proteases. 389 Mar 97
From a consideration of (varphi, Psi) values of the amino acids of myoglobin,
lysozyme
, the alpha and beta chains of horse oxyhemoglobin, tosyl-
alpha-chymotrypsin
, and carboxypeptidase A, an empirical procedure of predicting whether amino-acid residues in proteins are in a non-helical or may be in a helical conformation has been developed. The conformation of an amino acid at any position n is considered to be influenced by its nearest neighbors (the amino acids at positions n + 1 and n - 1), and the (varphi, Psi) values of the middle amino acid n for the various tripeptide sequences in the known proteins are tabulated. If helical, the (varphi, Psi) values are plotted to define a helical (varphi, Psi) domain. A 20 x 20 table for all tripeptides (n - 1)-(n)-(n + 1) taken sequentially for the entire chain was constructed; it lists the number of instances in which helical and non-helical conformations for the amino acids at position n were found. Certain sequences are found to be associated exclusively with non-helical and others exclusively with helical conformations, whereas many sequences may be either helical or non-helical. The distribution of non-helical residues serves to limit stretches of permissively helical regions; these are then further examined by the helical wheel method. As applied to cytochrome c from 18 species, the only permissively helical segment found was the stretch 91-101 near the C-terminus. For the variable regions of three light and three heavy chains of immunoglobulins, upper limits of 12 and 17% alpha-helix, respectively, were obtained.
...
PMID:An attempt to locate the non-helical and permissively helical sequences of proteins: application to the variable regions of immunoglobulin light and heavy chains. 410 30
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