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)

The synthesis of wild-type measles virus-specified polypeptides in Vero cells in pulse-chase experiments, in cells with synchronized protein synthesis by high salt concentration, and in the presence of proteolytic enzyme inhibitors was analyzed by polyacrylamide slab-gel electrophoresis. Six major (L, G, 2, NP, 5 and M) structural polypeptides were identified in infected cells. The results of pulse-chase experiments suggested that most of the structural polypeptides were synthesized at their final length. Polypeptide M was found to be sensitive to trypsin. In TLCK-treated cells its molecular weight was about 1000--2000 daltons higher than in untreated cells. A minor virus-specific polypeptide with a molecular weight of about 23,000 was found as a very faint and diffuse band. In addition, three nonstructural polypeptides with molecular weights of 65,000, 38,000 and 18,000 were also detected. The experiments with proteolytic enzyme inhibitors and with synchronized protein synthesis suggested that the polypeptide with a molecular weight of 65,000 might be a precursor of the structural polypeptide 5.
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PMID:Measles virus-specified polypeptides in infected cells. 11 24

In addition to the four major polypeptides VP1 and VP4, foot-and-mouth disease virus particles contain two minor polypeptides, mol. wt. 40 X 10(3) (P40) and 52 X 10(3) (P52). Extensive purification procedures failed to remove these minor polypeptides from the virus particles. Polypeptide P40 co-electrophoresed in SDS-polyacrylamide gels with VP0, the probable precursor of VP2 and VP4 and was inaccessible to iodination in situ. The second minor polypeptide, P52, co-electrophoresed with the virus infection associated (VIA) antigen found in large amounts in harvests of the virus grown in BHK 21 cells. Polypeptide P52 was shown to be located near the surface of the virus particle by iodination experiments and by its removal on incubating the particles with trypsin or chymotrypsin. Pactamycin mapping showed that this polypeptide was not a precursor of the structural polypeptides. About one copy of P52 and 4 copies of P40 were found in the virus particles sedimenting at 146S. However a larger number of copies was found in those virus particles sedimenting faster than the 146S peak.
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PMID:Characterization of the minor polypeptides in the foot-and-mouth disease particle. 17 28

A model of nucleosome is discussed, which consists of two nucleohistone strand folds, located at the same level, similarly directed and having a rhomboid form. The folds are symmetric to each other. Four histones (H3, H2a, H2b and H4) take part in the formation of each fold. Nucleosome begins with a DNA region, bound with H1 histone and terminates with free DNA. Total sequence of histones along DNA is H1-H3-H2a-H2b-H4-H4-H2b-H2a-H3. Polypeptide chains of neighboring histones are oppositely directed and are located at opposite DNA strands. The model explains regularities of chromatin splitting under combined effect of ds-nucleases and trypsin, and of ss-nucleases. It is also in a good agreement with other properties of chromatin. Nucleosomes join to each other "side-to-side" under coincidence of terminal elements with faces of the rhomboid nucleosome structures. The model permits to explain the formation of a highest order structure--a helix of six nucleosomes, forming a fibril of 250--300 A in diameter. The degree of DNA compactness in it reaches 80--100.
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PMID:[Planar model of nucleosome and chromatin structure of high orders]. 33 36

Maleilated histidine decarboxylase beta-polypeptide chain, containing 3 arginine residue, was hydrolysed by trypsin. 4 non-overlapping homogenous peptides were isolated, 3 of them containing one arginine residue and the 4th peptide being C-terminal fragment of beta-chain. beta-Polypeptide chain is found to consist of 78 amino acid residues and to have molecular weight of 8456. Primary structure of each peptide and their possible sequence in beta-chain are determined.
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PMID:[Amino acid sequence in tryptic peptides of maleylated Micrococcus sp. n. histidine decarboxylase beta-polypeptide chain]. 102 78

Macroscopic Na currents were recorded from N18 neuroblastoma cells by the whole-cell voltage-clamp technique. Inactivation of the Na currents was removed by intracellular application of proteolytic enzymes, trypsin, alpha-chymotrypsin, papain, or ficin, or bath application of N-bromoacetamide. Unlike what has been reported in squid giant axons and frog skeletal muscle fibers, these treatments often increased Na currents at all test pulse potentials. In addition, removal of inactivation gating shifted the midpoint of the peak Na conductance-voltage curve in the negative direction by 26 mV on average and greatly prolonged the rising phase of Na currents for small depolarizations. Polypeptide toxins from Leiurus quinquestriatus scorpion and Goniopora coral, which slow inactivation in adult nerve and muscle cells, also increase the peak Na conductance and shift the peak conductance curve in the negative direction by 7-10 mV in neuroblastoma cells. Control experiments argue against ascribing the shifts to series resistance artifacts or to spontaneous changes of the voltage dependence of Na channel kinetics. The negative shift of the peak conductance curve, the increase of peak Na currents, and the prolongation of the rise at small depolarization after removal of inactivation are consistent with gating kinetic models for neuroblastoma cell Na channels, where inactivation follows nearly irreversible activation with a relatively high, voltage-independent rate constant and Na channels open only once in a depolarization. As the same kind of experiment does not give apparent shifting of activation and prolongation of the rising phase of Na currents in adult axon and muscle membranes, the Na channels of these other membranes probably open more than once in a depolarization.
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PMID:Gating of Na channels. Inactivation modifiers discriminate among models. 243 40

The amino acid residues of spinach CF1 subunit delta are identified which are accessible and thus exposed within the quaternary structure of the ATP-synthase complex on the thylakoid membrane. Two types of antibodies in the monospecific polyclonal antiserum 306 against CF1 delta, described in the previous publication [Z. Naturforsch. 44c, 153-160 (1989)], were separated by virtue of their different affinity to thylakoid membranes and used for specific analysis of the products of proteolytic digestion of delta in situ. Polypeptide delta in situ, i.e. within the CF0 CF1 complex on the membrane, is not susceptible to digestion by aminopeptidase M and trypsin, but is shortened by about 1 kDa by carboxypeptidase Y and digested at residues Glu173 and Glu179 by the Staphylococcus aureus protease V8. The epitope on delta reacting with the agglutinating antibodies from serum 306 is lost after these proteolytical treatments and therefore situated on residues Met180-Val187. Since trypsin destroys this epitope only after prolonged incubation and with at least 50 micrograms trypsin/mg Chl, residue Lys169 of delta probably is inaccessible in situ. We conclude that the C-terminal amphipathic alpha-helix of spinach CF1 subunit delta is exposed on the thylakoid membrane, with the hydrophilic face directed to the outside, and that CF1 delta starts to be shielded within the quaternary structure of the CF0 CF1 complex between Glu173 and Lys169. The hydrophobic face of the c-terminal helix may be part of the binding surface towards CF0. Antibodies from serum 306 inhibit the PMS mediated cyclic photophosphorylation by reacting with C-terminal residues of delta.
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PMID:Localization and orientation of subunit delta of spinach chloroplast ATP-synthase within the CF0 CF1 complex. 2. Identification of C-terminal residues of delta, exposed on the thylakoid membrane. 247 16

Polypeptide fractions A-C (M.W., 7 kd, 4.7 kd, and 3 kd) were obtained from the primary culture supernatant of thymus epithelial cells from Wistar rats by high-pressure liquid chromatography with a gel-filtration column. Changes in the mitogen responses of rat thymocytes and their subpopulations with addition of a fraction were studied. One subpopulation was rich in non-rosette-forming cells (non-RFCs), and the other was cortisone resistant thymocytes (CRTs). These subpopulations were incubated with a fraction for 24 hrs. before mitogen stimulation. Fractions A and C increased the response of the non-RFCs to concanavalin A (Con A) and that of total thymocytes and CRTs to phytohemagglutinin (PHA). Fraction B inhibited Con A and PHA response of total thymocytes and CRTs. Fraction B was cytotoxic toward total thymocytes and CRTs when viability was evaluated by [3H]uridine prelabelling. This cytotoxicity was suppressed by treatment with trypsin. Subfractions B3 and B4 obtained by reversed-phase column chromatography were cytotoxic toward CRTs. The effects of the fractions on thymocyte maturation were different, showing their functional diversity.
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PMID:Functional diversity of polypeptides in primary culture supernatant of thymus epithelial cells. 262 4

The surface structure of foot-and-mouth disease virus (FMDV) and the interaction of the individual capsid proteins with the virus RNA have been examined using modification reagents. By measuring the extent of modification of the lysine residues of intact and disrupted virus particles and the 12S protein subunit with Bolton & Hunter reagent it was found that 54% of the residues of VP1, 15% of the residues of VP2 and 37% of the residues of VP3, equivalent to five, two and four lysine residues respectively, are on the surface of the intact virus particle. Polypeptide VP4 was not modified in intact virus particles, indicating that it has no lysine residues on the surface of the virus. Modification with sodium metabisulphite, which causes a specific transamination reaction between cytidylic acid residues in ssRNA and closely associated basic amino acids, cross-linked all four structural proteins to the virus RNA. Both fragments of VP1, produced by treatment of the virus particle with trypsin, are also cross-linked to the RNA. These observations have been combined with the evidence that the immunogenic activity of VP1 may be contained in two discontinuous sites, at amino acids 141 to 160 and 200 to 213, in proposing a model for the arrangement of this polypeptide in the virus particle.
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PMID:Surface structure and RNA-protein interactions of foot-and-mouth disease virus. 303 64

Polypeptide C (molecular weight 2640 Dalton) extracted from artificial gastric juice), copepsidyl (containing high dosage of pepsin) and panintestine (polyenzyme drug) are studied for their effect on the activity of digestive enzymes of glandular gastric element pancreas and small intestine of rats. It is established that all mentioned drugs stimulate enzymogenesis in the analyzed organs. The activity of pepsin increases in homogenates of gastric mucosa, the activity of trypsin, total proteinases, carboxypeptidase and amylase grows in pancreas homogenates, and that of leucineaminopeptidase--in small intestine.
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PMID:[Enzyme-forming function of digestive glands after administration of polypeptide C, copepsidyl and panintestine]. 309 69

Rat brain cortex, caudate nucleus and cerebellum contain one or more factors that confer Vasoactive Intestinal Polypeptide (VIP)-, dopamine (DA)- and norepinephrine (NE)-sensitivity to adenylate cyclase in the absence of added GTP. These factors also stimulate the basal activity of the enzyme. The activity is found in a 100 000 X g supernatant; has an apparent molecular weight greater than 450 000 daltons; is inactivated by pronase, alkaline phosphatase and ammonium sulphate, and partially degraded by trypsin; and is stable to heat and acidic treatment. The effect of the factors is additive with that of guanosine-5'-triphosphate (GTP), and is not abolished by guanosine 5'-0-(2-thiodiphosphate) (GDP-beta-S). These results suggest that stimulation of adenylate cyclase by VIP, and most likely by DA and NE, can be modulated by soluble proteins.
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PMID:Properties of cytosolic proteins that confer vasoactive intestinal polypeptide-sensitivity to rat brain adenylate cyclase. 664 95


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