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:3.4.21.4 (trypsin)
42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Lyophilized bovine, porcine, and human choroid plexuses contain .02-.09 U of antidiuretic activity per milligram. The antidiuretic factor in bovine choroid plexus was concentrated 100 times by extraction with acetic acid, fractional precipitation with acetone and ethyl ether, gel filtration, and paper chromatography. Resulting choroid plexus fraction IIgammaB2 was eluted from Sephadex G-25 in position corresponding to molecular weight between 750 and 3,500; its antidiuretic activity was destroyed by trypsin, performic acid, and thioglycollic acid, but was not affected by leucine aminopeptidase, carboxypeptidase A or B, or cyanogen bromide. HgammaB2 possesses antidiuretic, pressor, and oxytocic potencies (measured in anesthetized-hydrated rat, anesthetized rat, and isolated rat uterus, respectively) of 1.9, 0.5, and 0.1 U/mg, respectively.
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PMID:Antidiuretic peptide in mammalian choroid plexus. 81 22

A new, simple method has been developed for the purification of Streptomyces griseus trypsin [EC 3.4.21.4] from Pronase. Only a single operation of affinity chromatography on an agarose derivative, which was easily prepared by coupling a tryptic digest of salmine to cyanogen bromide-activated Sepharose 4B, was required. A high degree of homogeneity was demonstrated for the purified enzyme by disc electrophoresis, SDS-polyacrylamide gel electrophoresis and gel filtration, as well as by active-site titration. The behavior of a carboxypeptides B [EC 3.4.12.3]-like enzyme present in Pronase is also discussed.
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PMID:Affinity chromatography of trypsin and related enzymes. III. Purification of Streptomyces griseus trypsin using an affinity adsorbent containing a tryptic digest of protamine as a ligand. 81 28

A 4% cholesterol diet fed to rats for four weeks was found to increase the phospholipid and cholesterol contents and the activities of drug metabolizing enzymes in rat liver microsomes. Microsomes from rats on a high cholesterol diet were able to enhance the fluorescence of membrane bound 1-anilinonaphthalene 8-sulphonate (1,8-ANS) and ethidium bromide more than microsomes from rats on a standard diet. In the case of 1,8-ANS, the enhanced fluorescence was found to be due to the increased affinity of the molecules for microsomes. In the case of ethidium bromide the fluorescence increased partly because of the larger amount of binding sites and partly because of the enhanced quantum yield of the molecules. P-nitrophenol was found to compete with 1,8-ANS for the same binding sites in microsomes. On the other hand, 1,8-ANS lowered the rate of drug metabolism when present in the incubation mixture. In vitro treatments of microsomes with trypsin, phospholipase A or digitonin altered the binding properties of 1,8-ANS and ethidium bromide to microsomes. It is concluede that the binding sites of 1,8-ANS in microsomes are important for the activity of drug-metabolizing enzymes. The mechanisms of dietary cholesterol in enhancing the drug metabolism and the role of microsomal phospholipids in regulating the activity of drug-metabolizing enzymes are discussed.
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PMID:Dietary cholesterol caused modification in the structure and function of rat hepatic microsomes, studied by fluorescent probes. 82 81

During studies on the amino acid sequence of bovine nasal cartilage collagen, the cyanogen bromide peptide alpha1(II)-CB11 was degraded to smaller peptides with trypsin. One of the tryptic peptides, T5, which contained 39 residues was shown by amino acid and sequence analyses to occur in a predominant form that contained glutamine at position 5 and in a second form with leucine at this site. In addition to the heterogeneity at this position, amino acid analyses of five different preparations revealed that the peptide with leucine contained a seryl residue not found in the major form. Sequence heterogeneity at a third position of alpha1(II) was demonstrated by the isolation of a hexapeptide (T2) from the trypsin digest of alpha1(II)-CB11 which contained 0.21 residue of alanine and 0.77 of leucine. Both the leucine and alanine of T2 were removed after the second cycle of subtractive Edman degradation. These data show that at least two types of alpha1(II) chains, designated as alpha1(II)Major and alpha1(II)Minor, exist in bovine nasal cartilage. Further considerations suggest that these two chains are probably not variants derived from allelic genes but are the products of separate genes.
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PMID:The covalent structure of cartilage collagen. Evidence for sequence heterogeneity of bovine alpha1(II) chains. 83 47

The complete amino acid sequence of the coat protein of alfalfa mosaic virus (strain 425) is reported. Sequence determinations were mainly performed on peptides obtained from fragmentation by cyanogen bromide and trypsin. Both manual and automatic sequence methods were used. Some refinements of the solid-phase Edman degradation were introduced. The final alignment of the peptides was established by means of alternative cleavage methods, such as limited tryptic digestion of intact virus particles, tryptic digestion after blockage of lysine residues and chymotryptic digestion. The coat protein consists of 220 amino acid residues corresponding to a molecular weight of 24252. A remarkable clustering of basic residues occurs in the N-terminal part of the protein chain. Several internal hydrophobic clusters and a strongly acidic site at the C-terminus can be observed. Two regions of sequence homology (12 residues) were found. Some features of the secondary structure are predicted.
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PMID:Structural studies on the coat protein of alfalfa mosaic virus. The complete primary structure. 83 94

The complete primary structure of the major component myoglobin from the Arctic minke whale, Balaenoptera acutorostrata, was determined by specific cleavage of the protein to obtain large peptides which are readily degraded by the automatic sequencer. Over 80% of the amino acid sequence was established from the three peptides resulting from the cleavage of the apomyoglobin at the two methionine residues with cyanogen bromide along with the four peptides resulting from the cleavage of the methylacetimidated apomyoglobin at the three arginine residues with trypsin. The further digestion of the central cyanogen bromide peptide with trypsin and S. aureus strain V8 protease enabled the determining of the remainder of the covalent structure. This myoglobin differs from that of the dwarf sperm whale, Kogia simus, at 16 positions, and the common dolphin, Delphinus delphis, at 14 positions, from that of the common porpoise, Phocaena phocaena, and the bottlenosed dolphin, Tursiops truncatus at 13 positions, from that of the Amazon River dolphin, Inia geoffrensis, at 10 positions, and from that of California gray whale, Eschrichtius gibbosus, at 3 positions- All of the substitutions observed in this sequence fit easily into the three-dimensional structure of the sperm whale myoglobin.
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PMID:The complete amino acid sequence of the major component myoglobin from the arctic minke whale, Balaenoptera acutorostrata. 83 10

The complete amino acid sequence of the major component myoglobin from the dwarf sperm whale, Kogia simus, was determined by specific cleavage of the protein to obtain large peptides which are readily degraded by the automatic sequenator. Three easily separable peptides were obtained by cleaving the protein at its two methionine residues, and five peptides were obtained from the methyl acetimidated protein by cleavage with trypsin at the four arginine residues. Sequenator analysis of these fragments and the apomyoglobin provided over 80% of the covalent structure of the protein. The remainder of the primary structure was determined by further digestion of the two larger cyanogen bromide fragments with trypsin and staphylococcal protease. To reconfirm many of the substitutions found in this protein, the apomyoglobin was treated with 1,2-cyclohexanedione, and the resulting arginine protected protein was cleaved at its lysine residues with trypsin. This myoglobin differs from that of the sperm whale at 6 positions, and from the other cetacean myoglobins at about 16 positions. The appearance of a histidine residue at position 35 has no precedent in any myoglobin. The substitutions seen at positions 21, 51, and 132 are unique to date for cetacean myoglobins.
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PMID:The complete amino acid sequence of the major component myoglobin of dwarf sperm whale (Kogia simus). 84 20

The alfalfa mosaic virus protein was submitted to the action of cyanogen bromide. Four peptides were isolated. Study of these peptides allowed us to determine the order. Then protein was submitted, after S-carboxymethylation or S-aminoethylation, to the action of different proteolytic enzymes: trypsin, chymotrypsin, thermolysin and papain. The peptides issued from these different hydrolysis were separated on Dowex 50 X4 and Dowex 1 X2, and their amino acid composition was determined. The use of classical methods of sequence determination, of mass spectrometry and for one case the use of a sequencer, lead to the obtention of the primary structure of all the tryptic peptides. The studies of chymotryptic, thermolytic and papainic hydrolysates, and of cyanogen bromide rupture, allowed us to isolate the overlapping peptides which were necessary for the reconstitution of the complete proteic chain.
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PMID:[Determination of the primary structure of alfalfa mosaic virus (strain S) coat protein. II. Complete sequence of the protein (author's transl)]. 88 29

By combinations of selective chemical cleavage (cyanogen bromide), selective enzymatic cleavage (trypsin, thermolysin), and random cleavage (partial acid hydrolysis) a series of disulfide-containing peptides have been isolated from ovine lutropin beta subunit. These peptides suggest six disulfide linkages between half-cystine residues in positions 23-72, 26-110, 93-100, 34-88, 9-90, and 38-57. The latter pair was placed by elimination of other possibilities. The first three pairs are in agreement with a report by Chung, D., Sairam, M. R. and Li, C. H. (1975) Int. J. Peptide Protein Res. 7, 487-493; the pair 93-100 has also been detected by Reeve, J. R., Cheng, K. W. and Pierce, J. G. (1975) Biochem. Biophys. Res. Commun. 67, 149-155, using partial reduction and alkylation. In an attempt to improve the efficiency of enzymatic attack, a preliminary partial reduction as per Reeve et al. [16] was done. In this instance a peptide suggesting an additional disulfide linkage between half-cystines 23-26 was obtained as well as peptides consistent with the 23-72 and 26-110 placements. This was interpreted as an artifactual opening and recombining during partial reduction-reoxidation to produce the 23-26 linkage. The placement of three disulfide bonds (34-88, 9-90, and 38-57) is in disagreement with the pairings Chung et al. [15] suggest for these six half-cystine residues. Six reasons for uncertainty in the placement of disulfide bonds are discussed. It is concluded the definitive placement of the disputed three disulfide bonds in ovine lutropin beta subunit remains an open question.
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PMID:Studies of disulfide bond location in ovine lutropin beta subunit. 88 34

A phosphorylated polypeptide (E4) of molecular weight 5000-6000, has been isolated from bovine embryonic enamel by Bio-Gel P-10 gel filtration and DE-52 ion-exchange chromatography. The peptide contains three serine residues all of which are phosphorylated. All three O-phosphoserine residues are in glutamic acid-O-phosphoserine-tyrosine sequences that are distributed relatively evenly along the polypeptide chain. Although it was not possible to sequence the entire polypeptide chain directly by automatic peptide sequencing, a partial sequence and peptide map was constructed on the basis of the sequence and composition of peptides derived by cyanogen bromide, trypsin and chymotrypsin digestion. The presence of glutamic acid, tyrosine and leucine adjacent to and near the O-phosphoserine residues may be important in calcium binding and in mineralization.
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PMID:Isolation, characterization and partial amino acid sequence of a phosphorylated polypeptide (E4) from bovine embryonic dental enamel. 88 76


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