Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.3.1 (alkaline phosphatase)
 47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In a group of patients with endometriosis and in a control group of healthy women, the polymorphism of the following systems were studied: ABO and RH blood-group systems; serum proteins haptoglobin (HP), transferrin (TF), vitamin D-transporting protein (GC), protease inhibitor (PI), and the third component of the complement (C3); serum enzymes-amylase of the loci 1 and 2 (AMY1 and AMY2), pseudocholinesterase (E2), and alkaline phosphatase (PP); erythrocytic enzymes-acid phosphatase (ACP1), phosphoglucomutase (PGM1), superoxide dismutase (SOD-A), esterase D (ESD), and glyoxalase (GLO1). Statistically significant differences between the groups compared were established for five genetic systems: ABO, E2, C3, TF, and PGM1. Among patient with endometriosis, the rare alleles of the locus ESD-ESD5 and ESD7-were found, along with ESD 5-5 homozygotes. Several genetic loci can be involved in the pathogenesis of endometriosis; their products can be specifically realized due to peculiarities of biochemical reactions in the organisms of people predisposed to this pathology.
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PMID:[Genetic aspects of endometriosis: features of the distribution of polymorphic gene frequencies]. 910 63

Ten protein and enzyme polymorphic systems, viz. haemoglobin, albumin, transferrin, adenosine deaminase, adenylate kinase phosphoglucomutase, esterase-D, glyoxalase, alkaline phosphatase and amylase were studied in numigall (guinea fowl x chicken hybrids) to assess structural gene expression and regulatory gene divergence between the parental species. The investigation revealed presence of both the maternal and paternal electrophoretic components in case of adenosine deaminase, alkaline phosphatase, amylase, albumin and transferrin although no clear differences could be identified for haemoglobin and glyoxalase. Esterase-D and adenylate kinase phenotypes showed a dominance of the chicken type.
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PMID:Polymorphic protein expression (profile) in numigall. 913 79

Electrophoretic variation of enzymes in five Eimeria spp. of the domestic fowl, including nine strains, ten single-sporocyst clones and two single-sporozoite clones of E. acervulina, three strains each of E. maxima and E. tenella, two strains of E. praecox and one strain of E. necatrix, were assayed using cellulose acetate electrophoresis. Ten enzymes [aldehyde oxidase (AO), alkaline phosphatase (ALP), amylase (AMY), fumarate hydratase (FUM), glucose-6-phosphate dehydrogenase (G6PDH), glucose phosphate isomerase (GPI), glutamate-oxaloacetate transferase (GOT), isocitrate dehydrogenase (IDH), malate dehydrogenase (MDH) and phosphoglucomutase (PGM)] were analyzed for their ability to distinguish between these species and strains. Enzymatic activity of G6PDH, GPI, IDH, MDH and PGM was detected in all the Eimeria spp. examined. Strains within each species were characterized by the same electrophoretic variant of G6PDH. Electrophoretic variants of GPI and PGM were the most valuable in the identification of inter- and intra-specific variation, particularly in the field strains of E. acervulina and E. tenella. These two enzymes were used to examine single-sporocyst and single-sporozoite clones derived from two strains of E. acervulina. The enzymes in E. maxima appeared to be conserved, showing no variation among strains with the five enzymes detected. Relative mobilities, calculated as described in this paper, were found to be consistent between different electrophoresis runs and may serve as a reference when this medium is used.
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PMID:Isoenzymes of Eimeria from the domestic fowl: electrophoretic variants among species, strains and clones. 919 94

White New Zealand male rabbits were fed a high-cholesterol (1%) diet for 7 weeks. The activity of alkaline phosphatase (AP), alanine (AlaAT), aspartate (AspAT) aminotransferases and level of glucose in the blood plasma of rabbits was determined and compared with those of a control group of animals. The cholesterol-enriched diet resulted in increases in plasma AlaAT and AP activity and a decrease in plasma glucose. In the liver, cholesterol treatment decreased the activity of AspAT, AlaAT, AP, phosphoglucomutase, phosphofructokinase, pyruvate kinase and lactate dehydrogenase. Activities of glucosephosphate isomerase, aldolase and the level of glycogen were not affected. No statistically significant changes in the activity of examined enzymes in heart of rabbits fed with cholesterol-enriched diet were observed. Chronic intake of cholesterol in the diet had a negative effect on liver metabolism but not on heart metabolism in rabbits.
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PMID:Effect of cholesterol-enriched diet on liver and heart enzymes in male rabbits. 946 63

PP63 (parafusin) is a 63 kDa phosphoprotein, which exists in at least two different isoforms. It is very rapidly (80 ms) dephosphorylated during triggered trichocyst exocytosis. This occurs selectively in exocytosis-competent Paramecium tetraurelia strains. At least two protein kinases isolated from Paramecium, casein kinase type II kinase and cGMP-dependent kinase, are able to phosphorylate the two recombinant PP63/parafusin isoforms, both with phosphoglucomutase activity, in vitro. By performing mass spectrometric peptide mapping, we have investigated in vitro phosphorylation of recombinant PP63/parafusin by these kinases in comparison to in vivo phosphorylation of native PP63/parafusin isolated from Paramecium homogenates. Low picomolar quantities of proteolytic digests of recombinant and native PP63/parafusin, prior to and following alkaline phosphatase treatment, were directly analyzed by MALDI mass spectrometry. In native PP63-1/parafusin-1, six of 64 serine and threonine residues (S-196, T-205, T-280, T-371, T-373, and T-469) were found definitely, 27 were found possibly phosphorylated, 28 were identified as nonphosphorylated, and three were not covered by mapping. Three of the six certainly phosphorylated amino acids represent consensus phosphorylation sites for casein kinase II or cGMP-dependent protein kinase. In vitro phosphorylation studies of recombinant PP63/parafusin confirm that some of the sites found were used in vivo; however, also significant differences with respect to in vivo phosphorylation of native PP63/parafusin were observed. The two Paramecium protein kinases that were used do not preferably phosphorylate expected consensus sites in vitro. Homology structure modeling of PP63/parafusin with rabbit phosphoglucomutase revealed that the majority of residues found phosphorylated is located on the surface of the molecule.
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PMID:Comparison of in vivo and in vitro phosphorylation of the exocytosis-sensitive protein PP63/parafusin by differential MALDI mass spectrometric peptide mapping. 1038 18

Inhibitory activity directed against metalloenzymes has been highly purified from extracts of red kidney beans (Phaseolus vulgaris). The inhibitor is a substance of small molecular weight and appears to be a chelator of Zn(2+). One milligram of the preparation inhibited 23 milligrams carboxypeptidase A. The inhibitor also strongly inhibited carboxypeptidase B and alkaline phosphatase and could activate phosphoglucomutase that had previously been inactivated with Zn(2+). The isoelectric point of the inhibitor is 4.7. The inhibitor activity was abolished by preincubation with Zn(2+), Ni(2+), Co(2+), or Cu(2+). The mechanism of inhibition of carboxypeptidases and alkaline phosphatase by the bean inhibitor is apparently due to the complexing and complete removal of Zn(2+) from the enzymes.
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PMID:Metalloenzyme inhibitor from kidney beans: partial purification and characterization. 1666 Jul 67


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