Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0272170 (SDS)
 50,377 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. Non-collagenous substances in newborn calf dermis were extracted with solutions of various concentrations of MgCl2. The total protein and hydroxyproline contents in MgCl2 extracts increased with increase in the concentration of MgCl2 in the solutions. In particular, steep increases of their contents were observed at concentrations of MgCl2 from 0.5 to 1.0 M. Total amounts of hydroxyproline in 1.0, 2.0, and 3.0 M MgCl2 extracts were equivalent to 40-50% of the hydroxyproline content in the whole connective tissue. Hexose and hexosamine contents of MgCl2 extracts increased with increase of the MgCl2 concentration. Hexuronic acid was hardly present in the residues after extractions with 0.5, 1.0, 2.0, and 3.0 M MgCl2. 2. Plasma proteins, hyaluronic acid, and dermatan sulfate were extracted at low concentrations of MgCl2. A non-collagenous protein and MgCl2-soluble collagen were extracted with 1.0, 2.0, and 3.0 M MgCl2 solutions. The disperson of collagen fibrils was observed in the residue extracted with 1.0 M MgCl2 solution by electron microscopy; the fibril structure of collagen was disordered by extraction with 2.0 and 3.0 M MgCl2. The results suggest that the dispersion and disorder of collagen fibrils lead to the release of a non-collagenous protein. Furthermore, it is suggested that the removal of hyaluronic acid and dermatan sulfate was not very effective for the solubilization of a large amount of collagen, but was suitable as a pretreatment to the extraction of a non-collagenous protein accompanied by the solubilization of a large amount of collagen. 3. The non-collagenous protein was purified by DEAE-cellulose column chromatography. Polyacrylamide gel electrophoresis of this protein at pH 8.5 showed a single band moving to the cathode. The non-collagenous protein contained 3.7% hexose, 1.8% hexosamine, and no hexuronic acid. This protein is rich in glycine, glutamic acid, and alanine, and contains neither hydroxyproline nor hydroxylysine. Sedimentation analysis showed a single peak with 1.8 S and the molecular weight was approx. 43,000 as determided by SDS polyacrylamide gel electrophoresis.
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PMID:The removal of non-collagen components from newborn calf dermis with magnesium chloride solution. 0 51

Microorganisms capable of producing L-pyrrolidonecarboxylate peptidase [L-pyrrolidonyl peptidase, EC 3.4.11.8] were screened and a strain of Bacillus amyloliquefaciens was chosen as one of the most potent producers of the enzyme. The enzyme was purified from lysozyme-lysate of the bacterial cells by salting out with ammonium sulfate, adsorption on DEAE-cellulose, covalent chromatography on PCMB-Sepharose and by gel filtration on Sephadex G-150. By these procedures, the enzyme was purified about 800-fold with an activity recovery of 9%, and the preparation was electrophoretically homogenous. The enzyme was most active and stable at pH 7-8. The presence of 2-mercaptoethanol and EDTA was effective for stabilizing the enzyme. The molecular weight was estimated to be 72,000 by the gel filtration method and to be 24,000 by SDS-polyacrylamide gel electrophoresis, suggesting that the enzyme is a subunit oligomer, presumably trimer. The enzyme was inactivated by the addition of PCMB, sodium tetrathionate, Hg2+ and Cu2+, but the activity lost was restored by the addition of 2-mercaptoethanol and EDTA. The purified enzyme split amide and ester linkages in L-pyroglutamyl derivatives of L-alanine, beta-naphthylamine, alpha-naphthol, and 4-methylumbelliferone, but was completely inert towards various peptides and esters used as substrates for usual amino- and carboxy-peptidases, and for endopeptidases such as trypsin, subtilisin and alpha-chymotrypsin.
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PMID:Purification and characterization of L-pyrrolidonecarboxylate peptidase from Bacillus amyloiliquefaciens. 2 93

A neutral protease with kininogenase activity was isolated from human polymorphonuclear (PMN) leukocytes by cation exchange chromatography and gel filtration. The protease appears heterogeneous by cation exchange chromatography, isoelectric focusing and cationic disc gel electrophoresis, but homogeneous by gel filtration, sucrose density gradient ultracentrifugation, SDS-disc gel electrophoresis and immunoelectrophoresis. By carrying out the electrophoresis of the protease in acrylamide gels of varying concentrations, it was shown that they represent charge isomers. The protease was stable at pH 4-10, but labile to heat, being almost completely inactivated when incubated for 30 min at 70 degrees C. It exhibited proteolytic activity between pH 5 and 9, being maximal at 7.5-8.5. The molecular weight of the PMN protease was estimated to be about 20,000 daltons by gel filtration in aqueous buffer and about 26,000-28,000 daltons by SDS-disc gel electrophoresis and gel filtration in Sepharose 6B in the presence of the dissociating agent guanidine HCl. Its sedimentation coefficient was about 2.7S. Corresponding to the charge heterogeneity, by isoelectric focusing, the kinin-generating and esterolytic activities of the PMN granule lysate focused between pH 6.0 and 11.5, whereas the isolated PMN protease focused between 10.0 and 11.8. With respect to kinin generation, caseinolysis, and alanine esterase activity, the protease was inhibited by DFP and certain chloromethyl ketone inhibitors, as well as the plasma protease inhibitory a1-antitrypsin, a2-macroglobulin and antithrombin III. Both bradykinin and a methionyl-lysyl-bradykinin-like peptide were generated from highly purified kininogens by a lysosomal lysate containing the PMN protease. However, this assay was done with a crude enzyme preparation which contains an aminopeptidase capable of converting lysyl-bradykinin or methionyl-lysyl-bradykinin to bradykinin. When injected intradermally, the protease induced hyperemia, hemorrhage, and moderate enhancement of vascular permeability, but the mixture of the protease and kininogen induced a marked enhancement of vascular permeability.
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PMID:Neutral proteases of human PMN leukocytes with kininogenase activity. 5 89

By a mild alkaline treatment of pyocin R1, the core particle was released from the contracted sheath. After sucrose density-gradient centrifugation, core-rich fractions were treated with anti-sheath serum and by a second density-gradient centrifugation, purified core particles were isolated. Homogeneity of the preparation was confirmed by observation under the electron microscope, immuno-precipitation reaction, and sucrose density-gradient centrifugation. The core particle exhibited a sedimentation coefficient of 37S. The quaternary structure of the core consists of a single kind of subunit protein with a molecular weight of 18,000. No contamination by other proteins was detected by SDS-disc electrophoreses. Amino acid analysis revealed that the core is rich in glycine, alanine, valine, leucine, aspartic acid (or asparagine), glutamic acid (or glutamine), and serine. This amino acid composition bears some resemblance to that of T-even bacteriophage tail-core.
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PMID:Isolation, homogeneity, and properties of core particle from pyocin R1. 10 48

Pyruvate kinase isolated from Neurospora and purified to homogeneity has been shown to be a tetramer of molecular weight around 242 000 by gel filtration studies and 239 000 daltons by sedimentation equilibrium measurements. The monomer produced by treatment with guanidine hydrochloride is found to be 51 000-52 000 daltons by sedimentation equilibrium studies; a molecular weight of 62 000 was determined for the monomer generated by SDS treatment by electrophoresis in SDS-polyacrylamide gels. The enzyme has an isoelectric point of 6.35-6.41; Substrate saturation kinetics of PEP show a variable extent of cooperativity depending upon the buffer ions employed in the assay. ADP is the most effective phosphoryl group acceptor, GDP and IDP being poor substitutes. A divalent cation, Mg-2+, is required for activity. At low concentrations, Ca-2+ acts as an activator of pyruvate kinase but it is inhibitory at high concentrations. Fructose 1,6-diphosphate is the most potent allosteric activator, fructose 6-phosphate being next in order of effectiveness. Valine is a powerful inhibitor. Phenylalanine, tyrosine, and tryptophan are without any effect individually, but their simultaneous presence results in a considerable activation. Alanine does not affect this enzyme appreciably.
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PMID:Subunit structure and some properties of pyruvate kinase of Neurospora. 12 21

A lipophilic derivative of neocarzinostatin (NCS), an antitumor antibiotic, was prepared by reaction with a synthetic water-soluble polymer, [(styrene)1 approximately 3-(maleic acid 4 approximately 7/anhydride 1)]. The reaction was carried out at pH 8.6 for 3 h and aimed at modifying the two nonessential amino groups (alpha-amino of Ala-1, epsilon-amino of Lys-20). The NCS-polystyrene (SMANCS) was purified on a column of Sephadex G-100 in 0.05 M ammonium bicarbonate and the main product was obtained as a single peak. The elemental analysis showed an increased C and a decreased N content. U.v. and i.r. absorption spectra for SMANCS showed the presence of styrene. SDS-acrylamide gel electrophoresis at pH 8.5 and the decreased N content suggested a molecular weight of about 25 000, indicating the numbers of polymers conjugated to be about six units, two of which were found attached to the two amino groups. SMANCS was soluble in organic solvents, in contrast to NCS, and in water. SMANCS exhibited increased chemical and biological stability and appeared to possess similar in vitro biological activity.
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PMID:A lipophilic derivative of neocarzinostatin. A polymer conjugation of an antitumor protein antibiotic. 15 71

The protein moiety of squid (Watasenia scintillans) rhodopsin has been shown to have a molecular weight of 46 800 by means of amino acid analysis. This value was comparable to the value (51 000) obtained from SDS-polyacrylamide gel electrophoresis. After the squid eyes were incubated at 10 degrees C for 8 days, the rhodopsin showed a molecular weight of 39 000 on electrophoresis. The smaller molecular weight was ascertained by amino acid analysis of the rhodopsin; and may result from autolysis by the lysosomal enzyme. The rhodopsin in rhabdomeric membranes and in detergent solution was treated with chymotrypsin, papain or subtilisin. These enzymes first produced the 39 000 dalton rhodopsin and then cleaved this into the 25 000 and 14 000 dalton peptides without bleaching. The rhodopsin was attacked by proteases and readily lost an approx. 12 000 dalton peptide portion. This portion included the COOH-terminal and was rich in glutamic acid, proline, glycine, alanine and tyrosine residues.
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PMID:Molecular weight and structural studies on cephalopod rhodopsin. 46 26

PP10 was isolated from aqueous extracts of human term placentae by fractionating the proteins with rivanol and ammonium sulfate, by gelfiltration on Sephadex G-150 and by use of immunoadsorbents. PP10 apparently is a protein specific for the placenta; it could not be detected in extracts from other human tissues. From one human term placenta an average amount of 20 mg PP10 can be extracted. In sera from pregnant women PP10 is usually present only in trace amounts (less than 0.1 mg/100 ml). PP10 has the electrophoretic mobility of an alpha1-globulin and an isoelectric point of 5.1. The purified protein sediments with 3.8 S. PP10 was found to have a molecular weight of 48,000 as determined by ultracentrifugation and a molecular weight of 65,000 as determined by SDS-PAA gel electrophoresis. PP10 is a glycoprotein containing 6.65% carbohydrates (hexoses 4.8%, hexosamines 1.2%, fucose 0.05%, sialic acid 0.6%). The amino acid composition of PP10 has been determined, too; the most abundant amino acids in this protein are glutamic acid, aspartic acid, leucine and alanine.
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PMID:[Isolation and characterization of a new placenta specific protein (PP10) (author's transl)]. 48 20

Rates of protein synthesis by intact liver parenchymal cells isolated from male Fischer F344 rats ranging in age from 2.5 to 30 months were determined by measuring the incorporation of [3H] valine into acid-insoluble material and the specific activity of the extracellular valine. The rate of protein synthesis decreased 44% from 2.5 to 18 months and then increased slightly (18%) from 18 to 30 months. There was no dramatic change in the types of proteins synthesized by isolated liver parenchymal cells isolated from 2- or 18-month-old rats as determined by SDS-polyacrylamide gel electrophoresis. The ribosomal-transit time by liver parenchymal cells isolated from 18-month-old rats was 60% higher than the ribosomal-transit time of liver parenchymal cells isolated from 4-month-old rats. The fidelity of protein synthesis by parenchymal cells isolated from 4- and 18-month old rats was compared by measuring the incorporation of p-fluorophenyl alanine (an analogue of phenylalanine) into acid-insoluble material. Although protein synthesis decreased significantly from 4 to 18 months, the fidelity of protein synthesis remained constant.
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PMID:A comparison of protein synthesis by liver parenchymal cells isolated from Fischer F344 rats of various ages. 49 78

A simple and effective method to purify a phosphoprotein (B2) (Mr 68,000, pI 6.2-8) from phenol-soluble non-histone chromatin proteins of rat liver is described. The purification involved only two steps, CM-cellulose chromatography and preparative SDS/polyacrylamide (10%)-gel electrophoresis. The purified phosphoprotein B2 was shown to be homogeneous by SDS/polyacrylamide-gel electrophoresis. The yield was 2% of total non-histone chromatin proteins. The acidic to basic amino acid ratio of phosphoprotein B2 was less than 1, with high contents of glutamic acid, aspartic acid, arginine, lysine, glycine and alanine. The phosphate content of this protein is 0.3%.
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PMID:Purification of a phosphoprotein from chromatin of rat liver. 53 78


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