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

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

We studied the uptake of D-glucose and L-tryptophan by the small intestine and estimated the activities of the intestinal brush border enzymes (sucrase, lactase, NA+-K+-ATPase and alkaline phosphatase) and lysosomal enzymes in rats receiving T-2 toxin orally. considerable decrease occurred in glucose and tryptophan uptake and in brush border sucrase, lactase and (Na+-K+)-ATPase. Alkaline phosphatase activity and release of lysosomal enzymes (acid phosphatase and acid ribonuclease) was unchanged.
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PMID:Effects of T-2 toxin on glucose and tryptophan uptake and intestinal mucosal enzymes. 671 77

Simultaneous reduction in alkaloid yield and level of phosphatases by high concentrations of phosphate was observed in Claviceps sp. SD-58. Tryptophan-induced culture showed an increase in alkaloid yield and the level of phosphatases. Phosphate caused repression of both acid phosphatase (isoenzyme I) and alkaline phosphatase (isoenzymes III and V).
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PMID:Alkaloid production by Claviceps sp. SD-58; involvement of phosphatase isozymes. 683 54

Escherichia coli K-12, which is rich in alkaline phosphatase, exhibits phosphorescence characteristic of tryptophan at room temperature. E coli mutants which do not have alkaline phosphatase do not show long-lived phosphorescence. The phosphorescence spectrum and lifetime of E. coli K-12 was similar to that of purified alkaline phosphatase from E. coli. These results indicate that the long-lived tryptophan phosphorescence in E. coli is likely to be derived from alkaline phosphatase in situ. The temperature dependence of tryptophan phosphorescence life-time of purified alkaline phosphatase and E. coli K-12 differ; this may imply that alkaline phosphatase in E. coli may be associated with the cell envelope and is therefore protected against structural changes in the protein which result in increased phosphorescence decay rates.
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PMID:Phosphorescence of alkaline phosphatase of E. coli in vitro and in situ. 702 28

A new manganese-containing acid phosphatase has been isolated and crystallized from sweet potato tubers. The pure enzyme contains one atom of manganese per Mr = 110,000 polypeptide and shows phosphatase activity toward various phosphate substrates. The pH optimum of the enzyme was 5.8 and the enzyme activity was inhibited by Cu2+, Zn2+, Hg2+, AsO43-, and MoO42-. This stable metalloenzyme is red-violet in color with an intense absorption band at 515 nm (epsilon - 2460). Our electronic, circular dichroism, and electron spin resonance findings strongly indicate that the Mn-valence state of the native enzyme is trivalent. When the Mn-enzyme is excited by the 5145 A line of Ar+ laser, prominent Raman lines at 1230, 1298, 1508, and 1620 cm-1 were detected. This Raman spectrum can probably be interpreted in terms of internal vibration of a coordinated tyrosine phenolate anion. The tryptophan-modified enzyme showed a positive Raman band at 370 cm-1, which is preferentially assigned to a Mn(III)-S streching mode. The modification of the Mn-enzyme by N-bromosuccinimide led to a large decrease in the fluorescence intensity of 335 nm which was dominated by its tryptophan residues within a considerable hydrophobic environment. The acid phosphatase activity was significantly decreased by the tryptophan modification. With respect to the active site donor sets, the Mn(III)-containing acid phosphatase is distinctly different from the Zn(II)-containing alkaline phosphatase. Of interest is also the appreciable similarity of some enzymatic and spectroscopic properties between the present enzyme and uteroferrin.
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PMID:Purification, enzymatic properties, and active site environment of a novel manganese(III)-containing acid phosphatase. 728 28

D-penicillamine, an antirheumatic drug having chelating ability, was investigated for the effects on vitamin B6 and metals at doses ranging from 25 to 600 mg per kg, p.o., or in case of the highest dosing of D-penicillamine, together with s.c. administration of cupric sulfate or pyridoxine hydrochloride for 28 days in rats. The effects were compared with the actions of L- and DL-penicillamine. D-penicillamine increased urinary vitamin B6 excretion and lowered vitamin B6 levels extensively in serum and slightly in the liver. Those changes were also seen with L- and DL-penicillamine. On the other hand, D-penicillamine had no effects on the activities of serum transaminases and alkaline phosphatase and on the urinary excretion of xanthurenic acid after a tryptophan loading. D-Penicillamine, like L- and DL-penicillamine increased the urinary excretion of Cu and Zn and reduced Cu contents both in serum and liver. When Cu was given s.c. concomitantly with D-penicillamine p.o., an enhancement was seen in the effects of D-penicillamine on the urinary excretion of xanthurenic acid and body weight gain, as well as on the serum level of vitamin B6 and serum transaminase activities. Simultaneous injection of vitamin B6 with D-penicillamine produced a recovery in the lowering vitamin B6 levels induced by D-penicillamine in serum and liver and enhanced the urinary excretion of Cu, but did not influence the serum content of Cu. Thus, although the antivitamin B6 activity of D-penicillamine was demonstrated in rats, the degree was slight and was less than that seen with L- or DL-penicillamine. Moreover, the enhancing effect of Cu on the antivitamin B6 activity of D-penicillamine might be explained by the chelate formation between D-penicillamine-pyridoxal complex and Cu.
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PMID:[Effects of D-penicillamine on vitamin B6 and metal ions in rats (author's transl)]. 738 Mar 58

Weanling Wistar-strain female rats were fed a normal or an iron-deficient diet for 8 weeks and oral contraceptive steroids (OCS) were added for the last 4 weeks. Hemoglobin content, serum iron and zinc levels, liver iron levels, and tryptophan pyrrolase activities, and liver, kidney, and brain zinc levels and alkaline phosphatase activities were determined. Compared to control rats given the normal diet (N group), elevated liver zinc levels and tryptophan pyrrolase activity were found in rats fed the normal diet containing OCS ( + S group), but other parameters did not alter. In rats fed the iron-deficient diet alone (D group), only liver zinc levels were significantly higher, while other parameters were in general lower than those in the N group. In rats fed the iron-deficient diet containing OCS (D + S group), all hematological values, tissue mineral contents with the exception of liver zinc levels, and liver tryptophan pyrrolase and kidney alkaline phosphatase activities were lowered, compared to the N or N + S group. However, compared to the D group, the values of most parameters in the D + S group did not differ significantly, apart from an increase in serum zinc levels. These observations suggest that OCS does not greatly influence the various changes caused by iron-deficient anemia.
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PMID:Oral contraceptive steroids: effects on iron and zinc levels and on tryptophan pyrrolase and alkaline phosphatase activities in tissues of iron-deficient anemic rats. 738 13

A histochemical investigation has been made to localize and characterize various lipid, protein, carbohydrate and enzyme constituents present within the different cell types of the epidermis of Anabas testudineus. The polygonal cells contain glycogen, the amount of which gradually increases as the cells move towards the surface until they reach the most superficial layer where the amount of glycogen slightly decreases indicating the metabolically active state of these cells. The basal cells, which frequently undergo cell proliferation, contain no glycogen. The polygonal cells give strong reactions for SDH, alkaline phosphatase, cholesterol esters and nonsulphated acid mucopolysaccharides, moderate reactions for acidic lipids, phospholipids and free cholesterol and weak reactions for neutral mucopolysaccharides, protein bound NH2 groups, mucoprotein, tyrosine, tryptophan and cysteine bound sulphydryl groups. These cells in the outermost layer give stronger reactions for acidic lipids, phospholipids and cholesterol esters and weaker reactions for SDH and alkaline phosphatase activities. The above findings reveal that the polygonal cells remain metabolically active throughout the epidermis. The mucous cells are numerous and secrete mixture of neutral mucopolysaccharides, sulphated acid mucopolysaccharides and nonsulphated acid mucopolysaccharides. The contents of the sacciform granulated cels are mainly proteins. A thick coat of slime over the body surface containing mucopolysaccharides, lipids and proteins is important in keeping the skin moist and may facilitate the survival of the fish while it is on land. The melanophores in the epidermis may playing important role in preventing the colinization by parasites, fungi and bacteria over the body surface, act as macrophages.
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PMID:A histochemical study of the epidermis of the climbing perch, Anabas testudineus (Anabantidae, Pisces). 742 82

Placental alkaline phosphatase (PLAP) is initially synthesized as a precursor (proPLAP) with a C-terminal extension. We constructed a recombinant cDNA which encodes a chimeric protein (alpha GL-PLAP) comprising rat alpha 2u-globulin (alpha GL) and the C-terminal extension of PLAP. Two molecular species (25 kDa and 22 kDa) were expressed in the COS-1 cell transfected with the cDNA for alpha GL-PLAP. Only the 22 kDa form was labelled with both [3H]stearic acid and [3H]ethanolamine. Upon digestion with phosphatidylinositol-specific phospholipase C the 22 kDa form was released into the medium, indicating that this form is anchored on the cell surface via glycosylphosphatidylinositol (GPI). A specific IgG raised against a C-terminal nonapeptide of proPLAP precipitated the 25 kDa form but not the 22 kDa form, suggesting that the 25 kDa form is a precursor retaining the C-terminal propeptide. When a mutant alpha GL-PLAP, in which the aspartic acid residue is replaced with tryptophan at a putative cleavage/attachment site, was expressed in COS-1 cells, the 25 kDa precursor was the only form found inside the cell and retained in the endoplasmic reticulum, as judged by immunofluorescence microscopy. In vitro translation programmed with mRNAs coding for the wild-type and mutant forms of alpha GL-PLAP demonstrated that the C-terminal propeptide was cleaved from the wild-type chimeric protein, but not from the mutant one. This gave rise to the 22 kDa form attached with a GPI anchor, suggesting that GPI is covalently linked to the aspartic acid residue (Asp159) of alpha GL-PLAP. Taken together, these results indicate that the C-terminal propeptide of PLAP functions as a signal to render alpha GL a GPI-linked membrane protein in vitro and in vivo in cultured cells, and that the chimeric protein constructed in this study may be useful for elucidating the mechanism underlying the cleavage of the propeptide and attachment of GPI, which occur in the endoplasmic reticulum.
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PMID:Conversion of secretory proteins into membrane proteins by fusing with a glycosylphosphatidylinositol anchor signal of alkaline phosphatase. 751 12

The addition of excess Tb3+ to metal-depleted Escherichia coli alkaline phosphatase results in enhanced luminescence from enzyme-bound terbium, which increases with sample deoxygenation and exhibits a tryptophan-like excitation spectrum. Following pulsed excitation at 280 nm, the time-resolved terbium emission shows a negative prefactor associated with a submillisecond rise time, which is independent of the concentration of dissolved oxygen. The absence of a build-up phase and similarity in lifetime in the decay kinetics of directly excited (488 nm) terbium allows for the assignment of the submillisecond component in the 280 nm excited sample to bound terbium. The results of the steady state and time-resolved experiments suggest that the time evolution of alkaline phosphatase-bound terbium emission is determined by energy transfer (kET approximately 360 and 120 s-1) from the triplet state of tryptophan to terbium followed by terbium decay. This model is based on the observations that 1) the tryptophan phosphorescence lifetime (previously assigned to Trp109) corresponds to the longer component of the terbium emission and 2) the long-lived emission is enhanced, as is the Trp109 phosphorescence, by deoxygenation. An energy transfer mechanism involving the Trp109 triplet state is shown to be inconsistent with a dipole-dipole process and is best understood as a through-space electron exchange over a donor-acceptor distance of 9-10 A.
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PMID:Direct kinetic evidence for triplet state energy transfer from Escherichia coli alkaline phosphatase tryptophan 109 to bound terbium. 755 24

A ribozyme was constructed of the catalytic domain of tobacco ringspot virus satellite RNA and flanking sequences complementary to the target, secreted alkaline phosphatase (SEAP) mRNA. The ribozyme specifically cleaved the substrate in vitro; compared with that constant temperature. The relationship between specific endoribonuclease activity of the ribozyme and Mg2+ concentration was shown. The ribozyme was active in 293 cell line which was cotransfected with plasmids carrying the SEAP gene under control of RSV LTR promoter and the ribozyme gene under early HCMV promoter: SEAP activity reduced by half.
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PMID:[In vitro and in vivo study of the activity of secreted alkaline phosphatase mRNA ribozyme gene]. 773 97


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