Correction: Nucleotide and Amino Acid Sequences of Human Intestinal Alkaline Phosphatase: Close Homology to Placental Alkaline Phosphatase

1987 ◽  
Vol 84 (12) ◽  
pp. 4088-4088
Keyword(s):  
Alkaline Phosphatase ◽  
Amino Acid ◽  
Amino Acid Sequences ◽  
Placental Alkaline Phosphatase ◽  
Intestinal Alkaline Phosphatase

Differential regulation of mRNAs encoding for rat intestinal alkaline phosphatase

1990 ◽  
Vol 259 (1) ◽  
pp. G93-G98 ◽  
Author(s):  
R. Eliakim ◽  
S. Seetharam ◽  
C. C. Tietze ◽  
D. H. Alpers
Keyword(s):  
Alkaline Phosphatase ◽  
Amino Acid ◽  
Cdna Probe ◽  
Fold Increase ◽  
Maximal Activity ◽  
Amino Acid Residues ◽  
Intestinal Alkaline Phosphatase ◽  
Mrna Accumulation ◽  
Dihydroxyvitamin D3 ◽  
Fat Feeding

A cDNA probe encoding the entire structural region of the 62-kDa rat intestinal alkaline phosphatase from amino acid residues 1 to 531 detected multiple mRNA species (3.0, 2.7, and 2.2 kb) in rat intestinal RNA. The 3.0-kb species was most evident in duodenum but could be easily detected in jejunum using a 48-mer oligonucleotide encoding amino acid residues 492-508. This 48-mer oligonucleotide bound preferentially to the 3.0-kb mRNA, suggesting that the 2.7-kb mRNA differed in this region. To determine whether each of the mRNAs encoding rat intestinal alkaline phosphatase responded coordinately to physiological stimuli, the full-length cDNA and the 48-mer oligonucleotide were used as probes for the 2.7- and 2.2-kb and the 3.0-kb mRNAs, respectively. Intestinal mRNA concentration was measured by Northern blot analysis in acute (single feed, 17 kcal) and chronic (3 wk, 30% fat diet) fat feeding and in rachitic rats after 1,25-dihydroxyvitamin D3 therapy. There was a large increase (8- to 25-fold) in the 3.0-kb mRNA 7 h after acute fat feeding, with a much smaller increase (1.4- to 5.0-fold) in the 2.7- and 2.2-kb species. The peak in 3.0-kb mRNA accumulation correlated in time with the maximal activity of serum phosphatase activity after acute fat feeding (4- to 5-fold increase). In contrast, there was a much smaller increase in all mRNAs and in tissue and serum enzyme activity after chronic fat feeding.(ABSTRACT TRUNCATED AT 250 WORDS)

Macromolecular alkaline phosphatase and an immunoglobulin G that inhibited alkaline phosphatase in a patient's serum.

1983 ◽  
Vol 29 (2) ◽  
pp. 375-378 ◽  
Author(s):  
H Nakagawa ◽  
K Umeki ◽  
K Yamanaka ◽  
N Kida ◽  
S Ohtaki
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Immunoglobulin G ◽  
Significant Loss ◽  
Placental Alkaline Phosphatase ◽  
Type Ii ◽  
Intestinal Alkaline Phosphatase ◽  
Adult Type ◽  
Heat Stable

Abstract Macromolecular alkaline phosphatase (EC 3.1.3.1) was found in the serum of a patient suffering from myasthenia gravis (adult type II) complicated with thymoma, and was shown by immunoelectrophoresis to be bound to immunoglobulins A and G (IgG). Placental alkaline phosphatase, complexed with either the patient's serum or IgG purified from the patient's serum, remained at the origin on electrophoresis, with significant loss of activity. Intestinal alkaline phosphatase, complexed with either the patient's serum or the patient's IgG, migrated to a position similar to that of the macromolecular alkaline phosphatase in the patient's serum on electrophoresis. About 50% of the placental alkaline phosphatase activity was inhibited with 0.1-0.2 g of the patient's IgG per liter, but 6.93 g of the IgG per liter was required for about 20% inhibition of the intestinal alkaline phosphatase activity. The complex of intestinal alkaline phosphatase with the patient's IgG was fairly heat stable. From these results, we concluded that the macromolecular alkaline phosphatase in the patient's serum consisted of intestinal alkaline phosphatase and IgG that was specific for placental alkaline phosphatase.

scholarly journals Identification of Mimotope Peptides Which Bind to the Mycotoxin Deoxynivalenol-Specific Monoclonal Antibody

1999 ◽  
Vol 65 (8) ◽  
pp. 3279-3286 ◽  
Author(s):  
Qiaoping Yuan ◽  
James J. Pestka ◽  
Brandon M. Hespenheide ◽  
Leslie A. Kuhn ◽  
John E. Linz ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Alkaline Phosphatase ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Synthetic Peptide ◽  
Amino Acid Sequences ◽  
In Vitro Translation ◽  
Enzyme Linked Immunosorbent Assay ◽  
Translation System

ABSTRACT Monoclonal antibody 6F5 (mAb 6F5), which recognizes the mycotoxin deoxynivalenol (DON) (vomitoxin), was used to select for peptides that mimic the mycotoxin by employing a library of filamentous phages that have random 7-mer peptides on their surfaces. Two phage clones selected from the random peptide phage-displayed library coded for the amino acid sequences SWGPFPF and SWGPLPF. These clones were designated DONPEP.2 and DONPEP.12, respectively. The results of a competitive enzyme-linked immunosorbent assay (ELISA) suggested that the two phage displayed peptides bound to mAb 6F5 specifically at the DON binding site. The amino acid sequence of DONPEP.2 plus a structurally flexible linker at the C terminus (SWGPFPFGGGSC) was synthesized and tested to determine its ability to bind to mAb 6F5. This synthetic peptide (designated peptide C430) and DON competed with each other for mAb 6F5 binding. When translationally fused with bacterial alkaline phosphatase, DONPEP.2 bound specifically to mAb 6F5, while the fusion protein retained alkaline phosphatase activity. The potential of using DONPEP.2 as an immunochemical reagent in a DON immunoassay was evaluated with a DON-spiked wheat extract. When peptide C430 was conjugated to bovine serum albumin, it elicited antibody specific to peptide C430 but not to DON in both mice and rabbits. In an in vitro translation system containing rabbit reticulocyte lysate, synthetic peptide C430 did not inhibit protein synthesis but did show antagonism toward DON-induced protein synthesis inhibition. These data suggest that the peptides selected in this study bind to mAb 6F5 and that peptide C430 binds to ribosomes at the same sites as DON.

scholarly journals Site-specific mutations in the COOH-terminus of placental alkaline phosphatase: a single amino acid change converts a phosphatidylinositol-glycan-anchored protein to a secreted protein.

1992 ◽  
Vol 116 (3) ◽  
pp. 799-807 ◽  
Author(s):  
M E Lowe
Keyword(s):  
Amino Acids ◽  
Alkaline Phosphatase ◽  
Amino Acid ◽  
Cleavage Site ◽  
Single Amino Acid ◽  
Clotting Factor ◽  
Secreted Protein ◽  
Placental Alkaline Phosphatase ◽  
Hydrophobic Domain ◽  
Terminal Amino

Placental alkaline phosphatase (PLAP) is anchored in the plasma membrane by a phosphatidylinositol-glycan moiety (PI-glycan). PI-glycan is added posttranslationally to the nascent peptide chain after the removal of 29 amino acids from the COOH-terminus. The contribution of selected COOH-terminal amino acids to the signal for PI-glycan addition was tested by creating a fusion protein with the COOH-terminus of PLAP and a secreted protein and by mutagenesis of specific PLAP COOH-terminal amino acids. The cDNA encoding the COOH-terminus of PLAP was fused in frame to the cDNA for human clotting Factor X and expressed in transfected COS-1 cells. Fusion proteins containing 32 amino acids of the PLAP COOH-terminus were modified by PI-glycan addition. Thus, the signal for PI-glycan modification must reside in these amino acids. Next, the region between the hydrophobic domain and the cleavage site was examined for additional determinants. Mutations of the hydrophilic residues in the spacer region demonstrated that these amino acids do not contribute to the signal for PI-glycan addition. Deletion of amino acids in the spacer region prevented the addition of PI-glycan suggesting that the length of the spacer domain or the amino acids around the cleavage site are important determinants. Finally, we demonstrated that interruption of the hydrophobic domain by a charged residue prevents PI-glycan addition and results in a protein that is secreted into the medium. The finding that a single Leu to Arg substitution in the hydrophobic domain converts a PI-glycan anchored, membrane protein to a secreted protein suggests that an essential signal for the correct sorting of PI-glycan anchored proteins versus secreted proteins resides in the hydrophobic domain. Substitution of a charged amino acid for a hydrophobic amino acid may be a mechanism for producing membrane bound and secreted forms of the same protein.

scholarly journals Demonstration of species difference of placental alkaline phosphatase isozymes in acetone-fixed paraffin-embedded tissues.

1980 ◽  
Vol 28 (3) ◽  
pp. 282-284 ◽  
Author(s):  
K Dempo ◽  
R H Kottel ◽  
W H Fishman
Keyword(s):  
Heat Treatment ◽  
Alkaline Phosphatase ◽  
Amino Acid ◽  
Species Difference ◽  
Acid Inhibition ◽  
Placental Alkaline Phosphatase ◽  
Mouse Placenta ◽  
Human And Mouse

The best preservation and discrimination of alkaline phosphatase isozymes by means of amino acid inhibition and heat treatment was obtained in sections of acetone-fixed paraffin-embedded tissues as compared to tissues fixed either in 95% ethanol or standard formalin. The results are illustrated in a study differentiating the isozymes of human and mouse placenta.

Placental alkaline phosphatase as a tumor marker for primary intracranial germinoma

1988 ◽  
Vol 68 (5) ◽  
pp. 710-720 ◽  
Author(s):  
Jun Shinoda ◽  
Hiromu Yamada ◽  
Noboru Sakai ◽  
Takashi Ando ◽  
Toshifumi Hirata ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Tumor Marker ◽  
Cross Reactivity ◽  
Cyst Fluid ◽  
Enzyme Linked Immunosorbent Assay ◽  
Placental Alkaline Phosphatase ◽  
Intestinal Alkaline Phosphatase ◽  
Content Type ◽  
Intracranial Germinoma ◽  
Very High

✓ A sensitive enzyme-linked immunosorbent assay (ELISA) was used in a retrospective study of placental alkaline phosphatase (PLAP) levels in serum, cerebrospinal fluid (CSF), and intratumoral cyst fluid in primary intracranial germinoma. The ELISA showed no cross-reactivity with intestinal alkaline phosphatase except in very high concentrations, after samples had been heat-treated. Three patients with germinoma were studied for serum PLAP levels and in all the levels were elevated (3.78, 0.52, and 2.11 IU/liter). Two of the germinoma patients were studied for PLAP levels in the CSF, and both had elevated levels (0.83 and 9.83 IU/liter). The intratumoral cyst fluid in one case of germinoma was tested for PLAP and the level was found to be very high (603 IU/liter). These PLAP levels decreased concomitantly with the reduction in tumor size during irradiation. Serum PLAP levels were measured in 40 control adult male individuals and in the CSF of 20 nonpregnant patients with subarachnoid hemorrhage. The upper normal limits were 0.20 and 0.11 IU/liter in the serum and the CSF, respectively. All PLAP levels measured in the serum of patients with various brain tumors were 0.18 IU/liter or less. This study strongly suggests that PLAP is a clinically useful tumor marker for primary intracranial germinoma.

Rapid Communication: Ileal alkaline phosphatase is upregulated following functional amino acid supplementation in Salmonella Typhimurium-challenged pigs

2021 ◽  
Author(s):  
Lucas A Rodrigues ◽  
Michael O Wellington ◽  
J Caroline González-Vega ◽  
John K Htoo ◽  
Andrew G Van Kessel ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Amino Acid ◽  
Salmonella Typhimurium ◽  
Experimental Period ◽  
Post Inoculation ◽  
Adaptation Period ◽  
Intestinal Alkaline Phosphatase ◽  
Weanling Pigs ◽  
Plasma Alkaline Phosphatase ◽  
Dietary Treatments

Abstract We recently showed that functional amino acid (FAA) supplementation improves growth performance and immune status of Salmonella Typhimurium (ST)-challenged pigs which was further improved by a longer adaptation period. It is expected that the effects are associated with increased activity of intestinal alkaline phosphatase (IAP). The objective of this study was to evaluate the effects of FAA supplementation and adaptation period on the ileal, cecal, and colonic activity of IAP in weaned pigs challenged with ST. In Exp. 1, 32 mixed-sex weanling pigs were randomly assigned to dietary treatments in a 2 × 2 factorial arrangement with low (LP) or high protein (HP) content and basal (FAA–) or FAA profile (FAA+; Thr, Met, and Trp at 120% of requirements) as factors. In Exp. 2, a total of 32 mixed-sex weanling pigs were randomly assigned to 1 of 4 dietary treatments, being FAA- fed throughout the experimental period (FAA−) or a FAA profile fed only in the post-inoculation (FAA+0), for 1 wk pre- and post-inoculation (FAA+1), or throughout the experimental period (FAA+2). In Exp. 1 and 2, after a 7- and 14-d adaptation period, respectively, pigs were inoculated with saline solution containing ST (3.3 and 2.2 × 10 9 CFU/mL, respectively). Plasma alkaline phosphatase was measured on d 0 and 7 post-inoculation in Exp. 1, and IAP (ileum, cecum, and colon) was measured in Exp. 1 and 2. Correlations among ileal IAP and serum albumin and haptoglobin, plasma superoxide dismutase (SOD), malondialdehyde (MDA), and reduced:oxidized glutathione (GSH:GSSG), ileal myeloperoxidase (MPO), ST shedding and ileal colonization, and post-inoculation average daily gain (ADG), feed intake (ADFI), and gain:feed (G:F) were also analyzed. In Exp. 1, plasma alkaline phosphatase was decreased with ST inoculation and overall content was increased in LP-FAA+ compared to LP-FAA- (P < 0.05). Moreover, ileal IAP was increased in FAA+ compared to FAA- pigs in both studies (P < 0.05) regardless of adaptation time (P > 0.05). Intestinal alkaline phosphatase was positively correlated with MDA and ADFI and negatively correlated with SOD and ST shedding in Exp. 1 (P < 0.05). These results demonstrate a positive effect of FAA supplementation, but not adaptation period, on ileal alkaline phosphatase activity in Salmonella-challenged pigs, which may be associated with improvements in antioxidant balance.

Evaluation of Kinetic Enzyme Parameters by Use of a Small Computer Interfaced "Fast Analyzer"—An Addition to Automated Clinical Enzymology

1973 ◽  
Vol 19 (8) ◽  
pp. 908-918 ◽  
Author(s):  
T O Tiffany ◽  
D D Chilcote ◽  
C A Burtis
Keyword(s):  
Alkaline Phosphatase ◽  
Kinetic Parameters ◽  
Small Computer ◽  
Programming Approach ◽  
Initial Reaction ◽  
Placental Alkaline Phosphatase ◽  
Intestinal Alkaline Phosphatase ◽  
On Line ◽  
Clinical Enzymology ◽  
Glucose 6 Phosphate Dehydrogenase

Abstract The evaluation of steady-state enzyme kinetic parameters such as Km, Vmax, and Ki is useful in clinical enzymology, particularly where they can be used for the detection of enzyme variants and to assess the type of isoenzymes and the extent of their abnormal activity. The multiple-cuvet parallel-analysis feature of the Fast Analyzer permits one to evaluate one or more enzymic parameters in a single rotor. Both on-line measurement of initial reaction velocities and rapid off-line reduction of statistical data can be obtained by using the small-computer interfaced Fast Analyzer. Estimates of error in determining these parameters are also obtained, for use in comparing results in future analyses. We discuss the programming approach for adapting both simple and more complex statistical nonlinear regression data-fitting routines to the Fast Analyzer’s computer. We illustrate how the analyzer may be used to determine simple kinetic parameters for placental alkaline phosphatase and glucose-6-phosphate dehydrogenase and for the more complex "stripping out" of Km’s and Vmax’s for a heterogenous mixture of placental and intestinal alkaline phosphatase.

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