Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

---

Query: EC:3.1.3.1 (alkaline phosphatase)
47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A histochemical and autoradiographic study of the lining intestinal epithelium of the snake Xenodon merremii is reported. The absorptive cells present neutral polysaccharides, arginine, tyrosine, tryptophan, cysteine, alkaline phosphatase, acid phosphatase, ATPase, AMPase, esterase and RNA. There are histochemical differences between the goblet cells of the small and of the large intestine. Whereas in the former predominates the neutral polysaccharides and are found arginine, tyrosine, tryptophan and cysteine, in the latter predominates the sulfated polysaccharides (confirmed by the uptake of radioactive sulfur) and no amino acids were found.
...
PMID:Histochemical (polysaccharides, proteins, nucleic acids and enzymes) and autoradiographic (incorporation of 35S labelled sodium sulfate) study of the epithelial intestinal cells of Xenodon merremii Wagler, 1824 (Ophidia). 40 42

A simple inexpensive method has been developed for the synthesis of [2-3H]acetophenone, which has been converted into phenyl[2-3H]glyoxal. The latter compound has been used to modify arginine residues in alkaline phosphatase from two sources, and also a sialidase.
...
PMID:The synthesis of phenyl(2-3H)glyoxal. 42 78

Alkaline-phosphatase activity and the physico-chemical properties of the liver, lung, spleen, kidney, intestine, bone and placenta of 25 clinically healthy cattle and 30 clinically healthy sheep were investigated. High alkaline phosphatase activity was detected in kidneys and intestines. The alcaline phosphatase of cattle and sheep liver, spleen, kidney, lung, bone and placenta was thermo-labile and sensitive to l-arginine, l-homoarginine and imidazole, but was not sensitive to l-phenylalanine. Bone phosphatase of cattle and sheep was sensitive to urea. Intestinal phosphatase of cattle proved thermostable, sensitive to l-phenylalanine and not sensitive to l-arginine, l-homoarginine, imidasol and urea. Agarose gel electrophoresis of alkaline phosphatase indicated the presence of one fraction only and liver alkaline phosphatase proved to be the fastest. Sheep liver alkaline phosphatase had two fractions while sheep intestinal and placental alkaline phosphatase had three fractions and some of them were faster than liver alkaline phosphatase.
...
PMID:[Alkaline phosphatase activity and properties in the organs of cattle and sheep]. 54 64

A material identified as guanosine 5',3'-bis-diphosphate (ppGpp) has been detected in extracts of Chlamydomonas reinhardi ac-20 cells grown under mixotrophic conditions or in arg-2 cells deprived of arginine. The material was acid and base labile, susceptible to alkaline phosphatase, resistant to periodate oxidation, had spectral characteristics of a guanine derivative and comigrated on chromatograms with ppGpp from Escherichia coli. In ac-20 ppGpp may be involved in the control of chloroplast ribosomal RNA synthesis. When ac-20 cells were shifted from mixotrophic to autotrophic conditions, the 32Pi labeling of ppGpp, relative to that of GTP, was reduced, while the specific labeling of chloroplast ribosomal RNA was enhanced. Addition of low concentrations of cycloheximide had somewhat similar effects.
...
PMID:Synthesis of ppGpp and chloroplast ribosomal RNA in Chlamydomonas reinhardi. 62 52

Treatment of human prostatic acid phosphatase (orthophosphoric-monoester phosphohydrolase (acid optimum), EC 3.1.3.2) with either of the arginine-specific modifiers 2,3-butanedione or 1,2-cyclohexanedione in borate buffer at pH 8.1 leads to loss of activity. The inactivation by cyclohexanedione can be partially reversed by 0.2 M hydroxylamine. The rate of inactivation by both modifiers is decreased in the presence of the competitive inhibitors L-(+)-tartrate or inorganic phosphate but not in the presence of the non-inhibitor D-(-)-tartrate. Amino acid analysis of modified acid phosphatase indicates that only arginines are modified and that L-(+)-tartrate protects at least two arginyl residues from modification. A likely role of these arginyl residues is their involvement in binding the negatively charged phosphate group of the substrate.
...
PMID:An essential arginine residue in human prostatic acid phosphatase. 65 36

By means of CM-Sephadex column chromatography, Trimeresurus mucrosquamatus venom was separated into 20 fractions. Fraction XX had the marked anticoagulant action. This fraction was refractionated three times on Sephadex G-75, and a single peak was obtained. The patterns of microzone and disc electrophoresis also showed a single band. A single, symmetrical boundary with a value of 1.61 S was obtained by ultracentrifugation. It was a single peptide chain with a molecular weight of 11 700. The isoelectric point was higher than pH 10. The anticoagulant principle possessed phospholipase A activity and was calcium ion dependent. It did not possess proteolytic, tosyl-L-arginine methyl ester esterase, phosphodiesterase and alkaline phosphomonoesterase activities of the crude venom. The phospholipase A activity was heat-labile at pH 7.4, but was heat-stable at pH 5.6. The anticoagulant activity was more resistant to heat treatment as compared with phospholipase A activity. The anitoagulant action of the purified principle was competitively inhibited by platelet phospholid, tissue thromboplastin and cephalin, and was neutralized by antiserum. The anticoagulant principle inhibited platelet aggregation induced by ADP. It did not destroy fibrinogen, Factor X, prothrombin and thrombin; nor did it induce fibrinolysis nor interfere with the interaction between thrombin and fibrinogen. It is concluded that the anticoagulant action of this phospholipase A was due to the inhibition of the activations of Factors X and II through the inactivation of the procoagulant activity of phospholipids mediated partly by phospholipid-binding activity of this venom enzyme and partly by its enzymatic hydrolysis of phospholipids.
...
PMID:Purification and characterization of the anticoagulant principle of Trimeresurus mucrosquamatus venom. 66 29

Studied were the activity and properties of alkaline phosphatase (AP) in the seminal plasma, spermatozoa washed with physiologic saline, testes, and accessory sexual glands of a bull. The AP activity was highest in the seminal plasma (2493.2 IU/l) and lowest in the Kupffer gland (257.3 IU/kg crude tissue, on an average). In washed spermatozoa it proved by 10 per cent lower than the activity in seminal plasma. At 56 degrees C as much as 60-80 per cent of the AP in the investigated materials was inactivated for 30 min. AP was shown to be inactivated strongly (up to 84-97 per cent) by urea (3.8 M). L-arginine (10(-2) M) and EDTA (10(-3) M) inactivated to an equal extent AP in all studied organs. L-phenylalanine inactivated AP weakly (13-15 per cent) in the testis and the epididymis, and more strongly (32-57 per cent) in the accessory glands and the plasma. Agar electrophoresis revealed three to four isoenzymes of AP in the seminal plasma, three isoenzymes in the testis and the epididymis, and two isoenzymes in the accessory sexual glands and in spermatozoa washed with physioogic saline.
...
PMID:[Studies of the alkaline phosphatase in the sperm, testes and accessory sex glands of bulls]. 90 9

By means of DEAE-Sephadex A-50 column chromatography, Trimeresurus gramineus venom was separated into 12 fractions. Fraction 8 had marked anticoagulant action in the tests of whole blood clotting time, calcium clotting time and plasma prothrombin time. Fraction 8 was rechromatographed on Sephadex G-100, then on DEAE-Sephadex A-50 again, and finally on Sephadex G-100, and a single peak was obtained. The patterns of microzone and disc electrophoresis also showed a single band. A single symmetrical boundary with 1.70 Svedberg units was obtained by ultracentrifugation. The estimated molecular weight was 19 500. The isoelectric point was pH 4.5. Chemical analysis showed that the anticoagulant principle was a glycoprotein and that it was thermolabile. The anticoagulant activity of this purified principle was 3.5 times higher than that of the crude venom. Fraction 5 potentiated its anticoagulant activity to 10 times higher than that of the crude venom. This principle did not possess caseinolytic, tosyl-L-arginine methyl ester esterase, phospholipase A, phosphodiesterase, alkaline phosphomonoesterase, fibrinolytic, hemorrhagic or local irritating activities. The purified anticoagulant principle did not destroy fibrinogen, induce fibrinolysis, inactivate thrombin nor interfere with the interaction between thrombin and fibrinogen. However, a marked inhibition of prothrombin activation was caused by the anticoagulant principle. The inhibition of prothrombin activation was not due to the destruction of prothrombin or its activation factors, but due to an interference in the interaction between prothrombin and its activation factors because of the reversible binding of these factors with the anticoagulant principle of the venom.
...
PMID:Purification and properties of the anticoagulant principle of Trimeresurus gramineus venom. 113 81

Escherichia coli transports lysine by two distinct systems, one of which is specific for lysine (LysP) and the other of which is inhibited by arginine ornithine. The activity of the lysine-specific system increases with growth in acidic medium, anaerobiosis, and high concentrations of lysine. It is inhibited by the lysine analog S-(beta-aminoethyl)-L-cysteine (thiosine). Thiosine-resistant (Tsr) mutants were isolated by using transpositional mutagenesis with TnphoA. A Tsr mutant expressing alkaline phosphatase activity in intact cells was found to lack lysine-specific transport. This lysP mutation was mapped to about 46.5 min on the E. coli chromosome. The lysP-phoA fusion was cloned and used as a probe to clone the wild-type lysP gene. The nucleotide sequence of the 2.7-kb BamHI fragment was determined. An open reading frame from nucleotides 522 to 1989 was observed. The translation product of this open reading frame is predicted to be a hydrophobic protein of 489 residues. The lysP gene product exhibits sequence similarity to a family of amino acid transport proteins found in both prokaryotes and eukaryotes, including the aromatic amino acid permease of E. coli (aroP) and the arginine permease of Saccharomyces cerevisiae (CAN1). Cells carrying a plasmid with the lysP gene exhibited a 10- to 20-fold increase in the rate of lysine uptake above wild-type levels. These results demonstrate that the lysP gene encodes the lysine-specific permease.
...
PMID:The lysP gene encodes the lysine-specific permease. 131 32

TraC is one of the proteins encoded by the F transfer region of the F conjugative plasmid which is required for the assembly of F pilin into the mature F pilus structure. Overproduction of this protein from the plasmid pKAS2, which carries only traC, resulted in the formation of inclusion bodies from which soluble TraC was purified. When small amounts of TraC were produced from pKAS2, the protein was localized to the cytoplasm by using anti-TraC antibodies. Similar analysis of a set of TraC-alkaline phosphatase fusion proteins localized all of these fusion proteins to the cytoplasm. However, when TraC was expressed from the F plasmid, much of it appeared associated with the bacterial membrane fraction. Under these conditions, TraC does not appear to be part of the tip of the F pilus, as neither anti-TraC antibodies nor purified TraC had any effect on the infection of F-containing bacteria by the filamentous bacteriophage f1. These data suggest that TraC is normally associated with the membrane through interactions with other proteins specified by the tra region. This interaction may be via the carboxyl-terminal region of the TraC protein, as a mutant TraC protein containing an Arg-Cys substitution at amino acid 811 exhibits an interaction with the membrane weaker than that of the wild-type protein in the presence of the other Tra proteins.
...
PMID:Localization of TraC, a protein involved in assembly of the F conjugative pilus. 135 May 87


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>

---