Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.4 (trypsin)
 42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The single polypeptide chain of about 460 amino acids of porcine pancreatic lipase (EC 3.1.1.3) has been fragmented into five peptides by cyanogen bromide cleavage [Rovery, M., Bianchetta, J. & Guidoni, A. (1973) Biochim. Biophys. Acta, 328, 391--395]. The sequence of the first three cyanogen bromide peptides (CNI, CNII, CNIII), including a total of 234 amino acids, was fully elucidated. Automatic or manual Edman degradation was performed on the different peptides. Fragmentations of the CN peptides were accomplished by digestions with trypsin (after citraconylation or 1,2-cyclohexanedione treatment), chymotrypsin and Staphylococcus aureus external protease. Hydrolysis of unreduced material by pepsin and thermolysin, performed in order to determine the S-S bridge positions, provided useful overlapping peptides. The glycan moiety of lipase is bound to Asn-166. The non-essential tyrosine specifically blocked by diisopropylphosphorofluoridate is Tyr-49 in a cluster of asparagine and glutamine residues. The existence of a highly hydrophobic sequence (206--217) at the C terminus of the CNII fragment is noteworthy.
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PMID:Porcine pancreatic lipase. Sequence of the first 234 amino acids of the peptide chain. 38 Sep 92

The action of pepsin on the 11-S and 7-S proteins of vetch, 11-S protein of soybean and 7-S protein of Phaseolus vulgaris was investigated. The first three proteins are hydrolyzed almost completely, the rate of hydrolysis being close to that of hemoglobin, while the hydrolysis of Ph. vulgaris 7-S protein stops after the cleavage of only 2,4% of peptide bonds. The nonhydrolyzable high molecular weight core makes up to 87% of the initial protein and differs from the latter in its electrophoretic mobility and sedimentation coefficient. The action of pepsin does not increase the digestibility of Ph. vulgaris 7-S protein by trypsin. After the consecutive action of these enzymes about two thirds of the protein remain unhydrolyzed. The digestion of Ph. vulgaris 7-S protein by pepsin is completed only after its denaturation by heat treatment or by the action of 6 M guanidine hydrochloride.
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PMID:The action of pepsin on the reserve proteins of some leguminous seeds. 38 30

Ribosomal proteins S7 from 30S subunits of Escherichia coli strains K and B differ extensively in their aminoacid compositions. The experimental details which led to the determination of the complete primary structures of proteins S7K and S7B are presented. Protein S7K consists of a single polypeptide chain of 177 aminoacids giving a calculated molecular weight of 19, 732, whereas protein S7B has 153 residues which amount to a molecular weight of 17,131. Aminoacid sequences were determined by a combination of automated Edman degradation of the intact proteins in a modified Beckman sequenator and sequencing of peptides obtained by digestion with trypsin. Staphylococcus aureus protease, thermolysin and pepsin, either by solid-phase Edman degradation or by dansyl-Edman degradation. Additional information about the primary structure was derived from peptides resulting from chemical cleavages of the protein by 2-(2-nitrophenyl-sulphenyl)-3-methyl 3' bromoindolenine at its tryptophanyl bonds and by cyanogen bromide at its methionyl bonds leading to large fragments. The mutational event occurring between S7B and S7K was characterized. Protein S7K contains an additional sequence of 24 aminoacids at its C-terminal end. The aminoacid sequence of both proteins S7K and S7B was compared to the published sequences of the other ribosomal proteins of Escherichia coli and predictions for the secondary structure of these proteins were made.
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PMID:The primary structure of ribosomal protein S7 from E. coli strains K and B. 38 62

Homogeneous fragments of exosporium were isolated and purified from mature spores of a highly sporogenic mutant derived from Clostridium botulinum type A strain 190L. The exosporium was composed of three lamellae and showed a hexagonal array when negatively stained. The hexagonal array of isolated exosporium was resistant to sodium dodecyl sulfate, urea, dithiothreitol, and proteolytic enzymes such as trypsin, pronase, and nagarse, except for pepsin. The hexagonal array was partially disintegrated with 5 M guanidine-HCl and almost completely disrupted with 8 M urea in combination with 1% mercaptoethanol under alkaline conditions. The purified exosporium fraction was composed mainly of protein (69.1%) and lipids (13.8%). A small amount of amino sugars (2.5%) was present, but neutral sugars could not be detected. The exosporium protein had a predominantly acidic amino acid composition accompanied by low levels of cystine, methionine, and histidine.
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PMID:Isolation and partial characterization of exosporium from spores of a highly sporogenic mutant of Clostridium botulinum type A. 38 51

Human bile incubated with vitamin B12 bound to intrinsic factor in human gastric juice will effectively dissociate this complex, and the vitamin will transfer to non-intrinsic factor unsaturated binding protein(s) contained in bile. Preincubation of the bile with pancreatic enzymes, particularly trypsin, and pepsin, decreases this effect of bile on the intrinsic factor--vitamin B12 complex by digesting the unsaturated binder(s) in the bile. These studies help explain why there is malabsorption of tracer amounts of vitamin B12 in some patients with pancreatic insufficiency, and why this abnormality is correctable by the administration of pancreatic extract.
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PMID:Dissociation of the intrinsic factor--vitamin B12 complex by bile: contributing factor to B12 malabsorption in pancreatic insufficiency. 38 77

The primary structure of protein L21 from the 50S subunit of Escherichia coli ribosomes has been completely determined by sequencing the peptides obtained by digestion of L21 with trypsin before and after modification of the arginine residues with 1,2-cyclohexanedione, Staphylococcus aureus protease, thermolysin, and pepsin. Automated Edman degradation using a liquid-phase sequenator was carried out on the intact protein as well as on a fragment arising from cleavage with cyanogen bromide. Protein L21 consists of a single polypeptide chain of 103 amino acids of molecular weight 11 565. An estimation of the secondary structure of protein L21 and a comparison with other E. coli ribosomal protein sequences are presented.
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PMID:Amino acid sequence of the ribosomal protein L21 of Escherichia coli. 38 76

Protease inhibitors (inhibiting trypsin, chymotrypsin, and elastase) were demonstrated in human milk from birth to 4 months after delivery. No pepsin inhibitor was found. The protease inhibitors were localized in the alpha 1-region--inhibiting trypsin, chymotrypsin, and elastase--and in a more cathodal region--inhibiting chymotrypsin--in agarose gel electrophoresis of human milk. alpha 1-antitrypsin and antichymotrypsin were demonstrated by crossed immunoelectrophoresis. Electroimmunoassay showed the concentration of alpha 1-antitrypsin in 1st day milk to be 10.9% and the concentration of antichymotrypsin was 116% of that of adult serum. The concentrations decreased during the 1st wk; from 1 wk to 4 months they were 1.6% for alpha 1-antitrypsin and 3.8% for antichymotrypsin of those of adult serum. One ml of human milk from the first 3 days inhibits, by enzymatic methods, 0-150 microgram (mean value, 70 microgram) trypsin. Milk from 1 week after delivery and later inhibits 0-65 microgram (mean value, 38 microgram) trypsin per ml.
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PMID:Protease inhibitors in human milk. 38 34

The biological and immunological activities of Staphylococcal enterotoxin B are stable in pH 2.0 approximately 11.0, and also resistant to proteolytic enzyme (trypsin, pepsin) digestion for 3 approximate 4 hours. Therefore, the toxin could be purified with trypsin digest and then absorbed on kaolin and Kieselgel, followed by eluting the different pH buffer solutions. Further purifications was chromatographied on CM-Sephadex column.
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PMID:[Studies on staphylococcal enterotoxin B. III. Purification with absorbents]. 39 9

Immunohistochemical methods were employed for the investigation of bioptic and necroptic material fixed in formol and embedded in paraffin after it had produced very little or no fluorescence at all in the use of routine immunofluorescence techniques. Partial digestion with pepsin or trypsin or both enzymes in succession mostly facilitated positive immunohistological reaction. This particular procedure gives more scope to the methodological possibilities of histological material examination in that it offers an opportunity for the immunohistological investigation of even old material not specially preserved for immunohistological purposes but routinely fixed in ordinary formol. The simplification adds general availability to the method.
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PMID:[Immunofluorescence investigation of formol-paraffin material]. 39 44

Purified Streptomyces albus lytic enzyme was used in an attempt to extract type-specific antigen from a type 1, group A streptococcus. The presumably type-specific antigen was purified by ammonium sulfate fractionation followed by chromatography on O-(carboxymethyl)-cellulose columns. Comparison of the enzyme-extracted substance with acid-extracted material showed it to be serologically different from M protein. In addition, the extract obtained by enzyme treatment was resistant to trypsin as well as to the lytic enzyme. It was inactivated partially by pepsin and totally by papain. Comparison of the enzyme extract with pepsin-extracted T antigen showed these two preparations to be serologically identical. Subtle differences in their susceptibility to heat and acid treatment were noted. Immunodiffusion analyses of acid-extracted M protein and pepsin-extracted T protein, as well as with the enzyme extract, clearly established that the M-protein preparation contained a component serologically identical with one of the precipitinogens common to the other two extracts.
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PMID:Comparison of Streptomyces albus muramidase-extracted streptococcal antigen with acid-extracted M antigen and with pepsin-extracted T antigen. 40 3


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