Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

This paper reports on the concentration of total protein, reducing sugar, and various enzymes in uterine flushings obtained from 17 mature, regularly cyclic baboons and stored at -10 degrees C until required. It was found that the levels of total protein and reducing sugar was high at both the early proliferative and late secretory stages of the menstru al cycle and fell to their lowest levels in the early secretory phase. When an IUD was in situ, higher levels of these 2 constituents occurred. Of the enzymes measured in the early secretory phase, only hemoglobinase was significantly elevated in the presence of an IUD. Trypsin, chymotrypsin, lysozyme, amylase, and phosphatase were usually detectable in the flushes, but none was significantly altered by the device. The possible biologic implications of these findings are discussed.
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PMID:Studies on uterine flushings in the baboon. II. The effect of an intrauterine contraceptive device on certain biochemical parameters. 435 88

Trypsin- and chymotrypsin-treated delipidated cell walls of Mycobacterium smegmatis were digested overnight with lysozyme. The water-soluble products thus obtained were filtered on a column of Sephadex G-50; the first peak, excluded from the column, has immunological adjuvant activity. The material of the excluded peak is obtained after lyophilization as a snow-white, fluffy material, soluble in water and insoluble in organic solvents. It behaves as a slightly polydisperse macromolecule in an ultracentrifuge, with an approximate molecular weight of 20,000. All the constituents of this material are typical bacterial cell-wall constituents; thus, the water-soluble adjuvant is considered to be an "oligomer" of the cell wall. When added to Freund's incomplete adjuvant with an antigen (e.g., ovalbumin) and injected into hind-foot pads of guinea pigs, this water-soluble adjuvant increases the amount of precipitating antibodies and induces hypersensitivity to ovalbumin and the biosynthesis of gamma(2)-type precipitating antibodies. The water-soluble material has a stronger adjuvant activity than equal amounts of whole bacteria, cell walls, or wax D, and seems to be the first well-defined, water-soluble, adjuvant-active fraction isolated from Mycobacteria.
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PMID:Isolation and properties of a macromolecular, water-soluble, immuno-adjuvant fraction from the cell wall of Mycobacterium smegmatis. 450 37

1. With the aid of a coupled system involving glutathione reductase, the reaction of glutathione with the disulphide bonds of purified proteins has been studied. 2. Bovine serum albumin, conalbumin, lysozyme, trypsin inhibitors from egg white, lima bean and soya bean either did not react with glutathione or reacted only slightly. With these proteins reactivity was markedly increased by limited proteolysis. 3. Bovine and human gamma-globulins, fibrinogen and beta-lactoglobulin exhibited some reactivity (less than 15%) with glutathione and again this was increased by limited proteolysis. Pepsin, trypsin and chymotrypsin exhibited greater reactivity than the proteins previously mentioned. Di-isopropylphosphoryl-chymotrypsin exhibited less reactivity than chymotrypsin, suggesting that autolysis under the experimental conditions used contributed towards the reactivity of this protein. Proteolysis also increased the reactivity of these proteins. The three disulphide bonds of insulin were reduced by glutathione. 4. Above 35 degrees the disulphide bonds of serum albumin show a progressive increase in reactivity and at 55 degrees half of the bonds become accessible to glutathione. 5. From the results obtained with the proteins investigated, the conclusion reached is that the disulphide bonds of native proteins are structurally protected and do not react with glutathione under physiological conditions.
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PMID:The reactivity of the disulphide bonds of purified proteins in relationship to primary structure. 486 Apr 70

Satisfactory Raman spectra of crystalline lysozyme, pepsin, and alpha chymotrypsin were obtained with laser excitation. The spectra are very similar to each other, but show enough minor differences to make this a useful method of identification. The readily identified bands assignable to specific groupings are noted.
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PMID:Raman spectra of crystalline lysozyme, pepsin, and alpha chymotrypsin. 487 94

On the basis of earlier energy computations, the various single peptide units in proteins were designated as helix-making or helix-breaking.(1) With the use of these designations, empirical rules for distinguishing between alpha-helical and non-alpha-helical regions of proteins have been formulated. These rules include conditions for initiation and termination of a helical segment which, when combined with changes in the designation of three peptide units, correctly identify the helical or nonhelical character of over three fourths of the individual peptide units in four proteins of known amino acid sequence and structure: myoglobin, lysozyme, tosyl-alpha-chymotrypsin, and ribonuclease-A. The model is discussed, some of its predictions are checked, and further predictions about the structure of various proteins are made.
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PMID:The influence of short-range interactions on protein onformation. II. A model for predicting the alpha-helical regions of proteins. 525 50

It is shown that alpha-helical content of eleven proteins is well correlated with alanine plus leucine content. These residues, taken singly or together, are to a first approximation randomly distributed in the four proteins whose tertiary structures have been determined (i.e., myoglobin, lysozyme, ribonuclease, alpha-chymotrypsin). A model based on the concept that certain randomly distributed residues specifically participate in helix nucleation is shown to be in reasonable agreement with the presently published structures.
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PMID:A model of alpha-helical distribution in proteins. 569 10

Using ultracentrifugation, the systems of reversed micelles of aerosol OT in octane containing solubilized protein (alpha-chymotrypsin, lysozyme, trypsin, egg albumin, alcohol dehydrogenase from horse liver and gamma-globulin) were studied. The changes in the sedimentation coefficients of reversed micelles during incorporation of the protein are correlated (within a wide range of experimental conditions, e. g. degree of surfactant hydration or protein concentration) exclusively with the molecular weight of the solubilized protein. The simplest solubilization model, according to which the protein molecule is incorporated into the inner cavity of the reversed micelle at the stoichiometric ratio of 1 : 1, which does not affect the external sizes of the reversed micelle, has been proposed. Using alpha-chymotrypsin as an example, the conditions, under which the sedimentation properties of the systems deviate from this model, have been found. These deviations occurred at sufficiently low degrees of the surfactant hydration, when the inner cavity of the reversed micelle is smaller than the effective size of the solubilized protein molecule. In the latter case the protein forms a new micelle of necessary (i. e. larger) size. Since the hydrated micelle can be regarded as an elementary (30-100 A) fragment of biomembranes, the results obtained should be taken into consideration when analyzing the structural organization and functioning of the latter.
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PMID:[Enzymes incorporated into reversed micelles of surfactants in organic solvents. Study of the protein-aerosol OT-H2O-octane system by sedimentation analysis]. 617 48

The purpose of this study was to identify the fragment of the hen egg-white lysozyme (HEL) molecule presented by macrophages to helper T cells. This was investigated by using T-cell hybridomas and macrophages prefixed in paraformaldehyde. We previously had shown that such prefixed macrophages could present a tryptic digest of HEL. The tryptic peptides were separated by HPLC and tested for their ability to stimulate the T-cell hybridomas. Only one tryptic peptide was found to be immunogenic. This immunogenic peptide was identified as the tryptic peptide T-8, containing amino acids 46-61. The precise determinant on the peptide T-8 being recognized was further defined by testing the response of the two T-cell hybridomas to human lysozyme. Neither clone responded to human lysozyme. From the amino acid sequence of human lysozyme, the determinant was localized to the four amino-terminal residues. Cleavage of the immunogenic peptide with either chymotrypsin or protease V-8 completely abolished the immunogenicity. This suggested that the T-cell determinant is located in the hydrophilic amino-terminal residues and that it must be associated with a hydrophobic stretch of amino acids, which allows the peptide to associate with the macrophage plasma membrane.
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PMID:Processing of lysozyme by macrophages: identification of the determinant recognized by two T-cell hybridomas. 620 58

Since lysozyme and alpha 1-anti-chymotrypsin are constituents of normal histiocytes, their value as tumor cell markers in histiocytes neoplasias has been investigated using the indirect immunoperoxidase method and commercially available specific antisera on formaldehyde-fixed, paraffin-embedded 5 micrometers sections after pretreatment with pronase. The distribution of both markers was determined in 35 cases of malignant fibrous histiocytoma (MFH) and in 13 cases of malignant histiocytosis (MH). In 12 cases of MH both markers were found whereas in MFH alpha 1-antichymotrypsin was demonstrated in 26 and lysozyme in 16 cases only. In general, the staining for alpha 1-anti-chymotrypsin was more intense than the staining for lysozyme. A negative reaction does not exclude the possibility of MH or MFH. The presence of both constituents in tumours, however, can be considered as indicative of histiocytogenic origin and both can be useful markers for distinguishing histiocytic neoplasias from other tumours.
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PMID:Lysozyme (muramidase) and alpha 1-anti-chymotrypsin as immunohistochemical tumour markers. 628 96

Organic matter in sewage, soil, and aquatic systems may enhance or inhibit the infectivity of viruses associated with particulates (e.g., clay minerals, sediments). The purpose of this investigation was to identify the mechanisms whereby organic matter, in the form of defined proteins, affects the adsorption of reovirus to the clay minerals kaolinite and montmorillonite and its subsequent infectivity. Chymotrypsin and ovalbumin reduced the adsorption of reovirus to kaolinite and montmorillonite homoionic to sodium. Lysozyme did not reduce the adsorption of the virus to kaolinite, but it did reduce adsorption to montmorillonite. The proteins apparently competed with the reovirus for sites on the clay. As lysozyme does not adsorb to kaolinite by cation exchange, it did not inhibit the adsorption of reovirus to this clay. The amount of reovirus desorbed from lysozyme-coated montmorillonite was approximately 38% less (compared with the input population) than that from uncoated or chymotrypsin-coated montmorillonite after six washings with sterile distilled water. Chymotrypsin and lysozyme markedly decreased reovirus infectivity in distilled water, whereas infectivity of the virus was enhanced after recovery from an ovalbumin-distilled water-reovirus suspension (i.e., from the immiscible pelleted fraction plus supernatant). The results of these studies indicate that the persistence of reovirus in terrestrial and aquatic environments may vary with the type of organic matter and clay mineral with which the virus comes in contact.
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PMID:Effect of proteins on reovirus adsorption to clay minerals. 649 70


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