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 16 selected bacteriocins of Enterobacter cloacae were characterized presumptively. They proved to be noninfectious, sedimentable (105,000 X g), resistant against chloroform and trypsin, and nonfilterable. The host ranges were essentially species specific. Based on susceptibility to one or more of these 16 bacteriocins, 242 of 308 (78.6%) clinical E. cloacae isolates were typed and assigned to 52 provisional bacteriocin types. Several outbreaks of nosocomial cross-infection were discerned retrospectively. Thus, bacteriocin typing of E. cloacae isolates may prove useful for controlling hospital infection.
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PMID:Bacteriocin typing of clinical isolates of Enterobacter cloacae. 715 38

1. The possibility of stabilizing water-soluble enzymes against the inactivation action of organic solvents by means of surfactants has been studied. Several enzymes (alpha-chymotrypsin (EC 3.4.21.1), trypsin (EC 3.4.21.4), pyrophosphatase (EC 3.6.1.1), peroxidase (EC 1.11.1.7), lactate dehydrogenase (EC 1.1.1.27) and pyruvate kinase (EC 2.7.1.40)) were used to demonstrate that enzymes can be entrapped into reversed micelles formed by surfactants (Aerosol OT, cetyltrimethylammonium bromide, Brij 56) in an organic solvent (benzene, chloroform, octane, cyclohexane). The enzymes solubilized in this way retain their catalytic activity and substrate specificity. 2. A kinetic theory has been put forward that describes enzymatic reactions occurring in a micelle-solvent pseudobiphasic system. In terms of this theory, an explanation is given for the experimental dependence of the Michaelis-Menten equation parameters on the concentrations of the components of a medium (water, organic solvent, surfactant) and also on the combination of the signs of charges in the substrate molecule and on interphase (++, +-, --). 3. The results obtained by us may prove important for applications of enzymes in organic synthesis and for studying the state and role of water in the structure of biomembranes and active centres of enzymes.
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PMID:The principles of enzyme stabilization. VI. Catalysis by water-soluble enzymes entrapped into reversed micelles of surfactants in organic solvents. 721 47

Cytoplasmic membranes of L-forms of Staphylococcus aureus exerted a strong mitogenic effect on splenocytes of athymic nude mice as well as normal mice, while a cytoplasmic fraction of the same bacteria did not show definite mitogenicity. The mitogenic principle(s) of the membrane fraction was resistant to treatment with trypsin and was heat stable (at 100 C for 10 min). The active principle(s) in the insoluble residue of the membrane fraction digested with trypsin was not extracted with cold acetone, but could be solubilized by extraction with a cold chloroform-methanol mixture (2:1, v/v). The mitogenic principle(s) in the extract was fractionated by silicic acid column chromatography. Among five fractions separated by chromatography, fractions eluted with chloroform-methanol mixtures (1:1 and 1:20, v/v) were found to be strongly mitogenic. The cytoplasmic membranes of the L-forms also exerted a definite mitogenic effect on guinea pig splenocytes, but not on the thymocytes.
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PMID:Mitogenic activity of cytoplasmic membranes isolated from L-forms of Staphylococcus aureus. 721 5

G5-IgG is a monoclonal antibody that binds specifically to some cells and tissues of the adult rat nervous and immune systems. The molecular nature of the G5 antigen from adult rat brain is described in this paper. G5 antigen in adult rat brain membrane fractions was trypsin-sensitive and heat-labile but not chloroform/methanol-soluble. It was solubilized by the nonionic detergent NP40 but not by 3 M KCl. Detergent-soluble rat brain particulate protein inhibited G5-IgG binding to glutaraldehyde-fixed rat brain particulate protein. Inhibitory activity could be removed by prior incubation with concanavalin-A agarose beads. Immunoprecipitates of enzymatically iodinated, detergent-solubilized brain particulate protein gave a single band on polyacrylamide gels of apparent molecular weight 95,000--105,000 daltons. A band of identical molecular weight was visualized in gels of unlabeled immune precipitates by 125I-concanavalin A. These results strongly suggest that G5 is an integral membrane glycoprotein in adult rat brain.
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PMID:A new antigen common to the rat nervous and immune systems: II. Molecular characterization. 724 19

We have shown previously (D. A. Sirbasku, 1978, Proc. Natl. Acad. Sci. U.S.A., 75:3786-3790) that an estrogen-inducible growth factor activity for rat mammary and rat pituitary tumor cells can be identified in extracts of rat uteri, although at the time of that report only a limited biochemical characterization of the activity was presented. In this report, we have evaluated the growth factor activity for lipid, steroid hormone or protein-like properties. Uterine growth factor activity was assayed by measure of the increased cell number of the MTW9/PL rat mammary tumor cell line established by this laboratory and described previously (D. A. Sirbasku, 1978, Cancer Res. 38:1154-1165). Studies showed the following characteristics of growth factor activity: destroyed by trypsin treatment; labile when heated at 80 degrees C; partially denatured by 6 M guanidine or 8 M urea treatment or 50% aqueous solutions of organic solvents; inactivated by extremes of pH or overnight treatment with mild acid; not dialyzable at neutral pH; of apparent molecular weight of 70,000 daltons by G-100 Sephadex chromatography; possessing an isoelectric point of 4.8 to 5.2; not chloroform/methanol extractable; and not in any way identified as either a lipid or a steroid hormone. The data available suggest that the uterine growth factor activity is a protein or polypeptide of apparent high molecular weight, and that the activity does not directly correspond to other known growth factors.
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PMID:Properties of a growth factor activity present in crude extracts of rat uterus. 725 89

Capsular antigens were isolated from Pasteurella multocida, strain P-1059 and their immunogenicity was tested in turkeys. The crude capsular antigen (CCA) was extracted from bacterial cells grown on membranes by heating at 56 C in a 2.5% NaCl solution. The purified polysaccharide antigen (PPA) was obtained by precipitation of CCA by cetylpyridinium chloride. Young adult turkeys were inoculated at 0 and 14 days and were challenge exposed at 28 days by IM inoculation of a live culture of P-1059. The turkeys were observed for 2 weeks and mortality was recorded; bacterial isolation was done at the time of necropsy. In 3 trials, CCA provided 80% to 100% protection; in 1 trial, PPA failed to provide protection. Freund's incomplete adjuvant and aluminum hydroxide gel were effective as potentiating agents when higher than 280 microgram of CCA was used. The CCA showed significant (P less than 0.05) protection after treatment with heat (100 C, 5 min), chloroform, or trypsin, but lost its immunogenicity completely by acid hydrolysis. The CCA was not toxic to mice at 2 mg. The limulus lysate test showed that CCA contained endotoxin in less than or equal to 5% of the total solids. These results indicate that the surface antigen isolated from P multocida by saline extraction was immunogenic in young adult turkeys.
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PMID:Immunogenicity of capsular antigens of Pasteurella multocida in turkeys. 732 54

Cell-free wall, membrane, and cytoplasmic fractions were prepared from Bacillus sphaericus 1593, which exhibited toxic activity against larvae of the mosquito Culex pipiens var. quinquefasciatus. Breakage of 12- to 14-h cells by sonication or French pressure cell yielded toxic material which could be assayed in a standard mosquito larva bioassay. When sporulating cells of strain 1593 were fractionated, the majority of the toxic activity was localized in the cell wall rather than in the plasma membrane or cytoplasm. The toxin located in the bacterial cell wall was relatively stable, in that activity was unaffected by treatment with trypsin, pronase, CHCl3-CH3OH-water, Triton X-100, 8 M urea (30 min), heat (80 degrees C, 12 min), sonication, refrigeration, lyophilization, or freezing. Activity was destroyed by boiling for 10 min or by 0.01 N NaOH. Only about 1.0% of the activity present in purified cell walls could be recovered by a 2-h extraction with 8 M urea or 3 M guanidine hydrochloride. A comparison of the toxicity of a cell-free cell wall fraction with that of a sample consisting entirely of heat-stable spores indicated that the spore preparation was about 10 times more active.
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PMID:Localization of a mosquito-larval toxin of Bacillus sphaericus 1593. 740 88

A virus isolated in cell culture from the spleen of a cat with feline infectious peritonitis was identified by physicochemical, morphological and antigenic criteria as a coronavirus. The feline infectious peritonitis virus was compared in vitro with canine coronavirus, a reported enteric pathogen of dogs. The feline isolate was characterized, by chloroform sensitivity and resistance to 5-iododeoxyuridine, respectively, as containing essential lipid and an RNA genome. Other traits of the isolate included resistance to acidic conditions, heat lability, and resistance to trypsin. Electron microscopy showed viral particles with a structure consistent with that of the prototype of the coronavirus group, infectious bronchitis virus. Indirect immunofluorescence with canine coronavirus monospecific antiserum showed the viral isolate to be antigenically related to canine coronavirus. Specific-pathogen-free cats inoculated by various routes with cell-culture-propagated virus had both clinical symptoms and lesions consistent with feline infectious peritonitis.
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PMID:Characterization of a feline infectious peritonitis virus isolate. 746 85

Parathyroid hypertensive factor (PHF) has been purified from two sources of material: plasma of spontaneously hypertensive rats (SHRs) and culture medium from organ culture of SHR parathyroid glands. Chromatographic characteristics of PHF from these two sources are identical. Biological activity of PHF (assayed as the characteristic delayed hypertensive response in normotensive rats) is sensitive to degradation by treatment in base, and the enzymes trypsin, chymotrypsin, phospholipase C, and phospholipase D. PHF activity may also be extracted from source material with chloroform: methanol (4:1). A hypothetical structure for the active component of PHF is suggested. This is comprised of a peptide liked to a lysophospholipid.
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PMID:Purification and structural characterization of parathyroid hypertensive factor. 751 47

Carbohydrate epitopes of glycoconjugates are expressed on sensory neurons of dorsal root ganglion (DRG). A possible role of antibodies directed at carbohydrate determinants of the glycoconjugates has been suggested in some patients with sensory neuropathy. We investigated expression of blood group antigen-related epitopes in human DRG immunohistochemically using monoclonal antibodies to A, B, and H antigens. A blood group B determinant [Gal alpha 1-3(Fuc alpha 1-2)Gal beta-]-related glycoepitope was demonstrated in the neurons and surrounding satellite cells of DRG obtained from subjects with any ABO blood group phenotype. The treatment with trypsin or chloroform/methanol prior to the immunostaining suggested that the glycoconjugate exhibiting the blood group B determinant-related epitope consisted mainly of glycoprotein and included glycolipid. The glycoconjugates with the blood group B determinant-related epitope may play a role in the physiological function and pathophysiology of human DRG neurons.
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PMID:Expression of a blood group B antigen-related glycoepitope in human dorsal root ganglion cells. 753 59


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