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)

L-Tryptophan 2,3-dioxygenase (L-tryptophan: oxygen 2,3-oxidoreductase ( decycling ), EC 1.13.11.11) from Bacillus brevis, a moderately thermophilic bacteria, was purified to apparent homogeneity. The enzyme had a molecular weight of 110 000 and consisted of four subunits of equal molecular size. The enzyme exhibited the typical absorption spectra of a protohemoprotein . The amino acid composition and catalytic properties of the thermophilic enzyme were almost similar to those of its mesophilic counterpart from Pseudomonas acidovorans. However, the stabilities of the enzyme differed markedly between the two. The thermophilic enzyme was more resistant to heat and several chemical denaturants. The addition of L-tryptophan protected the enzyme from heat- and SDS- denaturations , and the tryptophan-mediated stabilization was more evident for the thermophilic enzyme. The effect of L-tryptophan on the stabilization of the thermophilic enzyme was more effective in preventing the dissociation of the tetrameric form of the enzyme (i.e. stabilizing it) in the case of the native, as compared to the mesophilic enzyme.
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PMID:L-tryptophan 2,3-dioxygenase of a moderate thermophile, Bacillus brevis. Purification, properties and a substrate-mediated stabilization of the quaternary structure. 671 60

Two serotypes of epidermolytic toxin were purified from culture filtrates of different strains of Staphylococcus aureus. The amino acid composition of the proteins is similar, each containing no cystine and one methionine, but type ii contains no tryptophan, whereas type i has 1 mol/mol protein. The molecular weights of type i and type ii toxins were 30,000 and 29,500, respectively, as found by SDS-polyacryamide gel electrophoresis and confirmed by studies of CNBr fragments and tryptic peptides. Dansylation gave a single different N-terminal amino acid for each toxin; the C-terminus of each is lysine. Peptide mapping of tryptic digests showed that very few peptides are common to the two amino acid sequences.
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PMID:A comparative study of two serotypes of epidermolytic toxin from Staphylococcus aureus. 677 85

Aminoacylase (EC 3.5.1.14) from Aspergillus oryzae was purified from a commercially available crude material by heat treatment, precipitation by polyethyleneimine and ammoniumsulfate, gel chromatography and preparative disc-gel-electrophoresis. The purified product was homogenous as judged by polyacrylamide gel electrophoresis. SDS-gel electrophoresis, polyacrylamide-gel-gradient electrohoresis, gel chromatography and amino acid analysis demonstrated the enzyme to be composed of two subunits with Mr of 36 600. The kinetic properties of the enzyme were studied with chloracetyl derivatives of alanine, phenylalanine, methionine, leucine, norleucine and tryptophan. The pH optimum of the acylase activity with chloroacetyl-alanine as substrate is at pH 8.5. Acyl derivatives of hydrophobic amino acids are preferred substrates. The enzyme has no dipeptidase activity. Aminoacylase is not inhibited by SH-blocking agents and no SH-groups could be detected with Ellman's reagent in the native and denatured enzyme. The enzyme activity is insensitive to phenylmethylsulfonyl fluoride and N-alpha-p-tosyl-L-lysine chloromethyl ketone. The microbial acylase is zince metallo enzyme. Mental chelating agents are strong inhibitors; it is further inhibited by Cd2+, Mn2+ and activated by Co2+. The properties of pig kidney and Aspergillus acylase are compared.
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PMID:Aminoacylase from Aspergillus oryzae. Comparison with the pig kidney enzyme. 677 95

The alpha and beta subunits of porcine FSH were isolated and purified to homogeneity as judged by SDS disc gel electrophoresis. The isolated subunits had less than 1% of the biological activity of the native hormone but were capable of recombining to generate at least 23% of the activity of the native hormone. The molecular weights calculated from hydrodynamic properties were 12,600 for pFSH alpha and 17,200 for pFSH beta. Total carbohydrate (g/100 g) was 18.9 for alpha and 15.1 for beta. The sialic acid content of alpha (3.8 g/100 g) exceeded that of beta (0.2 g/100 g). The alpha subunit contained significantly more lysine, alanine phenylalanine and methionine and significantly less aspartic acid, threonine, valine, isoleucine, leucine and tryptophan than the beta subunit. Evidence was found for N-terminal heterogeneity and an internal cleavage in the isolated alpha subunit.
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PMID:Isolation and characterization of the subunits of porcine follicle-stimulating hormone. 678 58

To further investigate the regulation of glucagon biosynthesis in mammalian A2-cells, we have studied the incorporation of [3H]-tryptophan into acid alcohol extracts of isolated pancreatic islets of guinea pig and mouse. Gel chromatography on Sephadex G-50 indicated that labelled proteins, migrating either with the void volume (peak I) or in region (peak II) between the void volume and the insulin marker, were formed during a 6h incubation of the islets. However, a period of at least two days in tissue culture was required before the islets showed any significant accumulation of labelled protein eluting in a position corresponding to that of pancreatic glucagon (peak III). Addition of glucose (16.7 mM) enhanced the incorporation into all chromatograph fractions during the culture period. Binding of gel chromatographed proteins Sepharose coupled anti-glucagon antibodies indicated that both guinea pig and mouse islets contained only small amounts of labelled, immunoreactive proteins eluting with either peak I or peak II. However, proteins eluting with peak III contained 6-8 times more lbelled, immunoreactive material than any of the other peaks. Total glucagon immunoreactivity was abundant in peaks I and II but less evident in peak II. The results of pulse-chase experiments provided no convincing evidence for a precursor-product relationship between larger proteins and glucagon. However, the heterogeneity of the putative precursor pool, as evidenced both by SDS-polyacrylamide gel electrophoresis and by the low immune binding, might have masked a conversion process. The combined data show that glucagon is, indeed, synthesized in isolated islets of guinea-pig and mouse, but that this process occurs slowly.
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PMID:Glucagon biosynthesis in isolated pancreatic islets of mice and guinea pigs. 699 3

Calmodulin has been isolated and characterized from the gill of the bay scallop aequipecten irradians. Quantitative electrophoretic analysis of epithelial cell fractions show most of the calmodulin to be localized in the cilia, specifically in the detergent- solubilized membrane-matrix fraction. Calmodulin represents 2.2 +/- 0.3 percent of the membrane-matrix protein or 0.41 +/- 0.5 percent of the total ciliary protein. Its concentration is at least 10(-4) M if distributed uniformly within the matrix. Extraction in the presence of calcium suggests that the calmodulin is not bound to the axoneme proper. The ciliary protein is identified as a calmodulin on the basis of its calcium- dependent binding to a fluphenazine-sepharose affinity column and its comigration with bovine brain calmodulin on alkaline-urea and SDS polyacrylamide gels in both the presence and absence of calcium. Scallop ciliary calmodulin activates bovine brain phosphodiesterase to the same extent as bovine brain and chicken gizzard calmodulins. Containing trimethyllysine and lacking cysteine and tryptophan, the amino acid composition of gill calmodulin is typical of known calmodulins, except that it is relatively high in serine and low in methionine. Its composition is less acidic than other calmodulins, in agreement with an observed isoelectric point approximately 0.2 units higher than that of bovine brain. Comparative tryptic peptide mapping of scallop gill ciliary and bovine brain calmodulins indicates coincidence of over 75 percent of the major peptides, but at least two major peptides in each show no near-equivalency. Preliminary results using ATP-reactivated gill cell models show no effect of calcium at micromolar levels on ciliary beat or directionality of the lateral cilia, the cilia which constitute the vast majority of those isolated. However, ciliary arrest will occur at calcium levels more than 150 muM. Because calmodulin usually functions in the micromolar range, its role in this system is unclear. Scallop gill ciliary calmodulin may be involved in the direct regulation of dyneintubule sliding, or it may serve some coupled calcium transport function. At the concentration in which it is found, it must also at least act as a calcium buffer.
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PMID:Specific localization of scallop gill epithelial calmodulin in cilia. 708 52

Chymotryptic subfragments from rabbit skeletal troponin T were purified using column chromatography. Molecular weight values on SDS gel electrophoresis, tryptophan contents, N- and C-terminal residues, and amino acid compositions were examined for each subfragment. Based on these findings, the positions of the subfragments in the sequence of troponin T were determined as follows: N-terminal acetylserine-1-tyrosine-158 for troponin T1 (MW 18,700); serine-156-C-terminal lysine-259 for troponin T2 alpha s (MW 12,200); leucine-159-C-terminal lysine-259 for troponin T2 (or troponin T2 alpha) (MW 11,900); leucine-159-phenylalanine-242 for troponin T2 beta I (MW 10,200); leucine-159-tyrosine-227 for troponin T2 beta II (MW 8,400); leucine-159-leucine-222 for troponin T2 beta III (MW 7,700); and serine-243-C-terminal lysine-259 for troponin T2 gamma (MW 1,800). The pathway of chymotryptic digestion of troponin T was also investigated and the results are discussed in relation to the higher structure of troponin T.l The interaction of some chymotryptic subfragments with tropomyosin was also investigated by affinity chromatography.
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PMID:Chymotryptic subfragments of troponin T from rabbit skeletal muscle. I. Determination of the primary structure. 709 86

Calcium binding protein (CaBP) has been reported to be involved in absorbing calcium in the duodenum. There is some evidence to show that active transport of calcium ions occurs from mother to fetus in the human placenta. The presence of CaBP in the human placenta was examined according to Taylor and Wasserman's method, extracting the vitamin D-dependent CaBP in the duodenum, and the character of CaBP was then studied. 38,000 X g supernatant of the villous homogenate of the human placenta was heated at 60 degrees C for 5 mins to neutralize the calcium binding activity resulting from the blood. The fractions containing CaBP were separated and partially purified on Sephadex G-100 and DEAE cellulose columns. The CaBP fractions were further purified by preparative agar electrophoresis. The Chelex-100-resin method was used for the detection of calcium binding activity in the eluates and for calculation of Kd values and of calcium binding sites. The molecular weights were determined by electrophoresis of SDS-polyacrylamide gel. Three CaBPs were found in the human placenta. The molecular weight, Kd (micro M) and the binding activity (Ca mol/CaBP mol) of the three placental CaBPs were CaBP-Peak I: 82,000, 0.64, 0.52; Peak II: 12,000, 0.67, 1.10; Peak III: 8,500, 0.75, 2.08, respectively. The tyrosine residue of CaBP has been shown to act as an important binding site in that removal of calcium ions from CaBP generates a blue-shifted phenomenon in the ultraviolet difference spectrum between 270 and 300 nm. However no difference spectrum was observed with the placental CaBPs. This result was further confirmed by amino acid analysis which showed that none of the placental CaBPs contained tyrosine, tryptophan, half-cystine and proline, which are usually found in most proteins. The circular dichronism (CD) spectrum of CaBP-Peak I in the far ultraviolet range showed two negative bands at 222 and 207 nm (alpha-helix structure), and removal of calcium ions caused no difference spectrum. CD spectra of CaBP Peak II and III in the far ultraviolet range revealed random coil structures in the presence and absence of bound calcium ions. These findings indicate that the calcium binding mechanism of the placental CaBPs should be different from that of the others. In this study, three kinds of human placental CaBP newly isolated were characterized according to molecular weights, Kd values and binding activities and clarified as having an amino acid composition quite different from the CaBPs already reported.
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PMID:[Characterization of the three calcium binding proteins in the human placenta (author's transl)]. 710 22

1. Scanning electron microscopy of minced dogfish, shark, and human lens fiber cell preparations showed that neither 8 M urea or 1% SDS was capable of totally disrupting the fiber cells, but that their membranes were totally disrupted by 1% SDS containing 50 mM dithiothreitol. 2. Fiber cells were purified by sucrose centrifugation and extracted with Tris-buffer, 8 M urea, 1% SDS and 50 mM dithiothreitol plus 1% SDS. 3. A residual 10% of the protein was capable of maintaining membrane integrity. 4. DTT + SDS totally dissolved the membranes, implying that disulfide bonds are involved in maintaining structure. 5. Non-tryptophan fluorescence was nearly totally extracted prior to the SDS-DTT step, indicating that the fluorescence associated with the membrane protein was not serving as crosslinks between extrinsic and intrinsic proteins. 6. Polyacrylamide slab gel electrophoresis revealed that after exhaustive extractions of lens fiber cells with Tris-buffer, 8 M urea and 1% SDS, the addition of DTT released major heat stable 27,000 and 24,000 dalton peptides. 7. The data support the concept that fiber cell membranes contain high levels of extrinsic peptides and intrinsic peptides whose stability depends strongly on oxidized crosslinks, probably disulfide bonds.
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PMID:Stability of shark and human lens fiber cell membranes. 715 18

The lactose-blockable lectin activity from fetal calf skeletal muscle has been purified to apparent homogeneity. The purification entails differential centrifugation, ammonium sulfate precipitation, asialofetuin affinity chromatography with a lactose gradient and ion-exchange chromatography on DEAE-cellulose. In the last step, the activity is resolved into a major and minor species, designated ion-exchange-purified lectins I and II, respectively. Both lectin activities are reversibly inhibited by lactose and appear as single bands with identical mobilities on SDS-polyacrylamide gel electrophoresis. Lectin II was not obtained in sufficient quantities for further characterization. Lectin I is characterized by a functional requirement for reducing agents and sensitivity to N-ethylmaleimide, which suggests a role for an essential thiol in its activity. Subunit molecular weight determinations by SDS-polyacrylamide gel electrophoresis (12 000 +/- 1 000) and by gel filtration in 6 M guanidine . HCl (13 000 +/- 1 000), when compared with that obtained under native conditions on Bio-Rad P-60 gels (27 000 +/- 2 000), suggest a true Mr of 25 000 +/- 3 000 for the dimeric molecule. Amino acid composition data, when fitted to this molecular weight, lead to the tentative conclusion that the intact dimer is composed of two very similar but compositionally non-identical chains, designated by alpha and beta. While the only detectable N-terminal amino acid is tryptophan, the isoelectric focusing pattern of lectin I supports this heterodimeric structure. In addition, a lactose-sensitive hemagglutinating activity which can be separated from the lactose-blockade activity by affinity chromatography was also observed.
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PMID:Physical and chemical characterization of the major lactose-blockable lectin activity from fetal calf skeletal muscle. 727 25


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