Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: Y22D7AL .14
 53,079 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Dopamine beta-hydroxylase (3,4- dihydroxyphenylethylamine ,ascorbate:oxygen oxidoreductase (beta-hydroxylating), EC 1.14.17.1) is the terminal enzyme in the biosynthetic pathway of norepinephrine. Chemical modification studies of this enzyme were executed to investigate contributions of specific amino-acid side-chains to catalytic activity. Sulfhydryl reagents were precluded, since no free cysteine residue was detected upon titration of the denatured or native protein with 2-chloromercuri-4-nitrophenol. Incubation of enzyme with diazonium tetrazole caused inactivation of the protein coupled with extensive reaction of lysine and tyrosine residues. Reaction with iodoacetamide resulted in complete loss of enzymatic activity with reaction of approximately three histidine residues; methionine reaction was also observed. Modification of the enzyme using diethylpyrocarbonate resulted in complete inactivation of the enzyme, and analysis of the reacted protein indicated a loss of approx. 1.7 histidine residues per protein monomer with no tyrosine or lysine modification observed. The correlation of activity loss with histidine modification supports the view that this residue participates in the catalytic function of dopamine beta-hydroxylase.
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PMID:Chemical modification of dopamine beta-hydroxylase. 672 74

Activation of bovine plasma prekallikrein was investigated with several proteinases. Highly purified bovine plasma prekallikrein was rapidly activated to kallikrein [EC 3.4.21.8] by bovine activated Hageman factor, trypsin [EC 3.4.21.4] and Pronase P (proteinases from Streptomyces griseus) and more gradually by papain [EC 3.4.22.2] and ficin [EC 3.4.22.3]. Activation of prekallikrein was also observed with bovine plasmin [EC 3.4.21.7], but not with bovine clotting factors Xa (Stuart factor) [EC 3.4.21.6] and IXa (Christmas factor) or thrombin [EC 3.4.21.5]. Urokinase [EC 3.4.99.26], Reptilase, collagenase [EC 3.4.24.3], elastase [EC 3.4.21.11], alpha-chymotrypsin [EC 3.4.21.1], Nagarse [EC 3.4.21.14], and stem bromelain [EC 3.4.22 4] did not convert prekallikrein to kallikrein. Plasma kallikrein activated to Hageman factor released kinin rapidly from bovine high molecular weight (HMW) kininogen. However, from bovine low molecular weight (LMW) kininogen, liberation of kinin was extremely slow. The kallikrein activity was inhibited by soybean trypsin inhibitor (SBTI), Trasylol, diisopropylfluorophosphate (DFP), and N-alpha-tosyl-L-lysine chloromethylketone (TLCK), but not by egg-white trypsin inhibitor (EWTI), lima bean trypsin inhibitor (LBTI), heparin or hexadimethrine bromide (Polybrene). The kallikrein formed an enzyme-inhibitor complex with SBTI and Trasylol, but not with LBTI. Prekallikrein did not react with SBTI. Prekallikrein consists of a single polypeptide chain of molecular weight about 90,000, as estimated by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis. Activation of prekallikrein by Hageman factor was found to involve cleavage of the single peptide bond on the disulfide-bridged polypeptide chain, and no change of molecular weight was observed during the activation. The peptide bond cleaved in prekallikrein by the activation was an Arg-X peptide bond on a disulfide-bridged polypeptide chain.
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PMID:Studies on prekallikrein of bovine plasma. II. Activation of prekallikrein with proteinases and properties of kallikrein activated by bovine Hageman factor. 676 24

The distribution in human tissues of enzymes which convert epsilon-N-trimethyl-L-lysine to L-carnitine was studied. Existing methodology was modified and new procedures were developed to measure enzyme activities. Epsilon-N-Trimethyl-L-lysine was converted to gamma-butyrobetaine in three enzymatic steps (hydroxylation at carbon 3, aldol cleavage between carbons 2 and 3 to yield glycine and gamma-trimethylaminobutyraldehyde, and subsequent oxidation of the aldehyde) in all tissues studied (liver, brain, kidney, heart and skeletal muscle), but gamma-butyrobetaine was hydroxylated to form L-carnitine only in liver, kidney and brain. Gamma-Butyrobetaine hydroxylase (4-trimethylaminobutyrate, 2-oxoglutarate: oxygen oxidoreductase (3-hydroxylating), EC 1.14.11.1) activity in liver was dependent on the age of the subject. The activity rose from 12% in infants to 100% of the adult mean by age 15 years. No age dependence could be demonstrated for the other three enzymes studied.
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PMID:Tissue distribution of carnitine biosynthetic enzymes in man. 677 Sep 10

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 influence was experimentally studied of different lysine and methionine amounts in pig rations on gain, blood picture and some blood serum biochemical indexes. A 95 per cent gain was recorded when 0.14 per cent Bulgarian lysine was added to the basal ration as against the group whose ration was supplemented by 0.20 per cent crystal imported lysine. Groups administered toxic lysine and methionine doses showed minimal gain or none. Blood serum Ca amount nearly doubled for groups showing excess of dietary lysine while P and M levels for the same groups appreciably dropped. Blood sugar level went up in methionine toxicosis.
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PMID:[Effect of various amounts of lysine and methionine on pigs]. 677 83

The pharmacokinetic study of a new analgesic-antiinflammatory agent, 2-(2'-methyl-3'-chloro-anilino)lysine nicotinate (L-104), was preformed in the rat and the dog. When administered p.o. in rats at a dose of 40 mg/kg, the serum peak was 131.3 microgram/ml +/- 10.3 at 15 min post application, and the elimination t 1/2 was 1.20 h. For the same dose, given i.v., the biological t 1/2 was 1.38 h, the AUC 337.18 microgram/ml/h and the Vdss 0.232 l/kg. When administered i.v. in dogs of 10 mg/kg, the biological t 1/2 was 0.96 h +/- 0.14, the AUC 73,066 microgram/ml/h and the Vdss 0.178 l/kg. In the rat, for a dose of 40 mg/kg given p.o., 79.1% of tritium-labelled L-104 were excreted within 72 h, 56.0% of them through the kidneys. In the dog, at an i.v. dose of 10 mg/kg, the whole of the drug was excreted at the end of 72 h, corresponding 52.6% urinary excretion. The main metabolite in the rat was 2-(2'-methyl-3'-chloro-4'-hydroxy-anilino)-nicotinic acid (72.2%), whereas in the dog it was 2-(2'-methyl-3'-chloro-anilino)-5-hydroxy-nicotinic acid (35.2%).
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PMID:Pharmacokinetic study of 2-(2'-methyl-3'-chloro-anilino)-lysine nicotinate (L-104). 679 66

Single cell protein (SCP) derived from secondary clarifiers of pulp mills is a potential commercial protein supplement in many areas. Samples of SCP were collected from several pulp mills in the Pacific Northwest and evaluated by laboratory procedures. Six in vivo digestion trials were conducted to determine the relative nutritive value of SCP that was dewatered by centrifugation or by the addition of a polyacrylamide polymer before being put through a belt press and dried with a sonic dehydrator. Amino acid analyses showed that SCP was higher in methionine than was cottonseed meal (CSM) and had a similar level of lysine. True protein, based upon amino acids recovered in SCP samples, ranged from 51.6 to 65.9% of the crude protein (CP). Pepsin digestibility of the CP ranged from 16.2 to 36.8%. Pepsin digestibility increased by 6.3 to 11.3 percentage units when SCP were incubated in a buffered rumen fluid for 24 hours. Solubility of the nitrogenous components in 10% Burroughs' buffer solution ranged from 12.4 to 36.5%. The range in mineral composition was : P, .62 to 1.55%; Ca, .14 to .99%; K, .21 to 5.52%; Mg, .07 to .59%. The concentration of trace minerals and heavy metals varied considerably from sample to sample. Digestion trials were conducted with sheep to compare SCP with CSM; 20 to 50% of the total CP was provided by the SCP sources. The CP digestibilities of the centrifuged and the polymer-dewatered SCP were 70.5 to 70.8% and 66.3 to 69.9%, respectively, of that observed for CSM. In all digestion trials, sheep consumed the SCP diets readily, and no digestive disturbances were observed. On the basis of laboratory and in vivo results, pulp mill SCP has the potential to be a viable protein supplement for livestock.
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PMID:Evaluation of single cell protein from pulp mills: laboratory analyses and in vivo digestibility. 680 31

We have characterized the UDP-galactose: alpha-N-acetylgalactosaminide beta 3 galactosyltransferase in human tracheal epithelium using asialo ovine submaxillary mucin as the acceptor. Maximal enzyme activity was obtained at pH 6.0-7.5 and at 20-25 mM MnCl2 and at 2% Triton X-100. Cd2+ could substitute for Mn2+ as the divalent ion cofactor. Spermine, spermidine, putrecine, cadaverine, and poly-L-lysine stimulated the enzyme activity at low (2.5 mM) MnCl2 concentration. The apparent Michaelis constants for N-acetylgalactosamine, asialo ovine submaxillary mucin, and UDP-galactose were 15.5, 1.14, and 1.36 mM, respectively. The enzyme activity was not affected by alpha-lactalbumin. The alpha-N-acetygalactosaminide beta 3 galactosyltransferase was shown to be different from the N-acetylglucosamine galactosyltransferase by acceptor competition studies. The product of galactosyltransferase was identified as Gal beta 1 leads to 3GalNAc alpha Ser (Thr) by (a) isolation of [14C]Gal-GalNAc-H2 after alkaline borohydride treatment of the 14C-labeled product, (b) establishment of the beta-configuration of the newly synthesized glycosidic bond by its complete cleavage by bovine testicular beta-galactosidase, and (c) assignment of the 1 leads to 3 linkage by identification of threosaminitol obtained from the oxidation of the disaccharide with periodic acid followed by reduction with sodium borohydride, hydrolysis in 4 N HCl, and analysis on an amino acid analyzer. The 1 leads to 3 linkage was confirmed by its resistance to jack bean beta-galactosidase and by the presence of a m/e 307 ion fragment and the absence of a m/e 276 ion by gas-liquid chromatography-mass spectrometry analysis. When acid and beta-galactosidase-treated human tracheobronchial mucin was used as the acceptor, 3.3% of the product was found as [14C]Gal-GalNAc-H2. The remainder of the [14C]Gal was found in longer oligosaccharides formed by a different beta-galactosyltransferase. This galactosyltransferase is slightly inhibited by alpha-lactalbumin and stimulated by spermine.
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PMID:Mucin biosynthesis. Characterization of UDP-galactose: alpha-N-acetylgalactosaminide beta 3 galactosyltransferase from human tracheal epithelium. 680 62

A method for the specific determination of a form of alpha 2-antiplasmin which does not interact with the lysine-binding sites in plasminogen (NPB-AP) has been elaborated. Basically, the method is an electroimmnoassay utilizing an intermediate gel, which adsorbs the plasminogen-binding form of alpha 2-antiplasmin (PB-AP). The plasma concentration of NPB-AP in healthy individuals was determined as 0.40 mumol/1 +/- 0.14 (SD), constituting 35% +/- 11 (SD) of the total plasma alpha 2-antiplasmin concentration. During extensive plasmapheresis of two pregnant severely D-immunized women the NPB-AP form decreased significantly, while the PB-AP form increased, thus maintaining the total alpha 2-antiplasmin at an almost constant level. The increased biosynthesis rate of alpha 2-antiplasmin during the extensive plasmapheresis is thus accounted for by PB-AP indicating this form to be the one primarily synthesized and that the non-binding form is formed in plasma from PB-AP secondarily.
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PMID:Studies on a form of alpha 2-antiplasmin in plasma which does not interact with the lysine-binding sites in plasminogen. 681 54

Six varieties of triticale and two varieties of wheat flours were analyzed for their proximal composition. The protein content of triticale flours ranged from 7.2 to 11.0%, and that of wheat flours, was 10.8 and 10.9%, respectively. The biological quality of Tca 8-74, measured as PER in Wistar rats, was 1.14, while that of commercial wheat flour was 0.85 (P less than 0.05). Amino acid supplementation of triticale flour with 0.2% L-lysine or 0.4% DL-threonine did not improve the biological quality of the protein. Supplementation with both amino acids, however, significantly improved both weight gain and PER. The value for the latter was 2.59 as compared to 2.62 for the standard casein diet. A panification assay was carried out using triticale, wheat and triticale: wheat blends in the following proportions: 1:0; 3:1; 1:1; 1:3; 0:1, and all of the breads were tested for their PER in rats. The PER for wheat bread and triticale bread was 1.05 and 1.25, respectively. None of the breads made from the wheat and triticale blends improved its protein quality beyond that of the wheat or triticale breads. The results of this study indicate that triticale has a better protein quality than wheat; furthermore, it may be used either alone or mixed with wheat in panification without affecting its protein value.
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PMID:[Chemical and nutritional evaluation of triticale (Secale sp.) cultivated in Chile]. 717 Dec 84


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