scholarly journals Identification of Rat Serum Alkaline Phosphatase Isoenzyme by means of Wheat Germ Agglutinin.

1997 ◽  
Vol 46 (1) ◽  
pp. 89-92 ◽  
Author(s):  
Hiroshi WADA ◽  
Noboru NIWA ◽  
Takashi HAYAKAWA ◽  
Haruhito TSUGE
Keyword(s):  
Alkaline Phosphatase ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Serum Alkaline Phosphatase ◽  
Rat Serum ◽  
Alkaline Phosphatase Isoenzyme

Alkaline phosphatase isoenzyme reactivity with wheat-germ agglutinin.

1986 ◽  
Vol 32 (2) ◽  
pp. 402-403
Author(s):  
B Desoize ◽  
L Cravero ◽  
J C Jardillier
Keyword(s):  
Alkaline Phosphatase ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Alkaline Phosphatase Isoenzyme

scholarly journals Reaction Rate Retardation as a Method for Serum Alkaline Phosphatase Isoenzyme Measurement

1980 ◽  
Vol 17 (4) ◽  
pp. 192-198 ◽  
Author(s):  
Pamela B Brown ◽  
K O Lewis
Keyword(s):  
Alkaline Phosphatase ◽  
Reaction Rate ◽  
Serum Alkaline Phosphatase ◽  
Enzyme Reaction ◽  
Intestinal Alkaline Phosphatase ◽  
Wide Range ◽  
Alkaline Phosphatase Isoenzymes ◽  
Sensitivity And Selectivity ◽  
Rate Retardation ◽  
Alkaline Phosphatase Isoenzyme

A method for serum alkaline phosphatase isoenzymes using an enzyme reaction rate analyser is described. The complete urea-induced degradation of enzyme activity is monitored, from which individual isoenzyme activities are obtained by calculating the constituent exponential components of the degradation curve. Activities have been measured with adequate sensitivity and selectivity for up to four isoenzyme components in normal and in pathological sera. The identity of each isoenzyme present is assigned from its characteristic degradation half-life, and by this method bone and liver alkaline phosphatase are clearly distinguished and quantitated, and a composite value for placental-intestinal alkaline phosphatase activity is obtained. The approach promises to be applicable to a wide range of isoenzymes, and in analogy with ‘reaction rate’ the term ‘reaction rate retardation’ is suggested for the procedure.

THE EFFECTS OF SOME DIETARY DERIVED LIPIDS AND FAT SOLUBLE VITAMINS ON RAT SERUM TRIBUTYRINASE AND ALKALINE PHOSPHATASE

1952 ◽  
Vol 30 (4) ◽  
pp. 308-313
Author(s):  
Jack D. Taylor ◽  
Neil B. Madsen ◽  
Jules Tuba
Keyword(s):  
Fatty Acids ◽  
Alkaline Phosphatase ◽  
Oleic Acid ◽  
Stearic Acid ◽  
Serum Alkaline Phosphatase ◽  
Adult Rats ◽  
Rat Serum ◽  
Low Levels ◽  
Fat Soluble Vitamins ◽  
Increased Activity

Synthetic diets were fed to adult rats for four weeks to determine the effects of dietary stearic acid, oleic acid, glycerol, Crisco, and vitamins, A, D, and E on the activity of serum alkaline phosphatase and serum tributyrinase. On a diet devoid of fats or fatty acids, the rats manifested abnormally low enzyme levels, which for serum alkaline phosphatase fell to values characteristic of starvation. Basal levels of the two enzymes, obtained with a fat free diet, were not altered by the ingestion of glycerol or vitamins A, D, and E. Dietary stearic acid, oleic acid, and Crisco, each significantly increased activity of phosphatase and tributyrinase and it would appear that both enzymes are concerned with intestinal absorption of fatty acids. The effect of oleic acid was most pronounced with both enzymes. The rats all gained weight during the tests so none of the variations in enzyme levels can be attributed to inanition. After the dietary test periods, all groups were starved for one week. Serum phosphatase values fell to the same constant low levels for all animals. Tributyrinase values rose towards levels which suggest that the enzyme is concerned with mobilization of depot fats during periods of fasting.

scholarly journals Immunoadsorption assay for bone alkaline phosphatase compared with wheat germ agglutinin precipitation assay in serum from (pre)pubertal girls

1996 ◽  
Vol 42 (12) ◽  
pp. 1970-1974 ◽  
Author(s):  
A A Bouman ◽  
C M de Ridder ◽  
J H Nijhof ◽  
J C Netelenbos ◽  
H A Delemarre-vd Waal
Keyword(s):  
Alkaline Phosphatase ◽  
Correlation Coefficient ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Bone Alkaline Phosphatase ◽  
Cross Reactivity ◽  
Reference Ranges ◽  
Correlation Studies ◽  
Deming Regression ◽  
The Mean

Abstract The performance characteristics of two bone alkaline phosphatase (ALP; EC 3.1.3.1) assays, a wheat germ agglutinin (WGA) precipitation assay and a new immunoadsorption assay (IAA), were compared. The within- and between-run imprecision of the IAA (3.6-4.2% and 3.6-7.7%) was comparable with that of the WGA assay. The mean cross-reactivity with liver ALP appeared to be 4% in the WGA assay and 11% in the IAA. The reference ranges in a group of 155 healthy Caucasian (pre)pubertal schoolgirls were: 149-401 U/L (total ALP, 30 degrees C), 105-349 U/L (bone ALP, 30 degrees C, WGA assay), and 58-205 U/L (bone ALP, 25 degrees C, IAA). Comparison of the WGA assay (x) with the IAA (y) demonstrated a correlation coefficient of 0.95 [Deming regression equation: y = (0.56 +/- 0.01)x + (2.0 +/- 1.5); Sy[symbol: see text]x = 5.3 U/L]. Correlation studies of the WGA assay and the IAA results with total ALP demonstrated r = 0.98 and 0.96, respectively.

Serum alkaline phosphatase isoenzyme activities in canine malignant mammary neoplasms with and without osseous transformation

2006 ◽  
Vol 35 (3) ◽  
pp. 287-290 ◽  
Author(s):  
M. Karayannopoulou ◽  
Z. S. Polizopoulou ◽  
A. F. Koutinas ◽  
A. Fytianou ◽  
N. Roubies ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Serum Alkaline Phosphatase ◽  
Mammary Neoplasms ◽  
Alkaline Phosphatase Isoenzyme

Wheat germ lectin affinity electrophoresis of serum alkaline phosphatase with commercially available agarose gels

1993 ◽  
Vol 39 (7) ◽  
pp. 1404-1407 ◽  
Author(s):  
M Mattiazzo ◽  
I Ramasamy
Keyword(s):  
Alkaline Phosphatase ◽  
Wheat Germ ◽  
Serum Alkaline Phosphatase ◽  
Single Step ◽  
Agarose Gels ◽  
Lectin Affinity ◽  
Affinity Electrophoresis ◽  
Alkaline Phosphatase Isoenzymes ◽  
Electrophoresis Method ◽  
Wheat Germ Lectin

Abstract We have modified a commercially available procedure involving precast agarose gels (Paragon Isopal System) to measure alkaline phosphatase (EC 3.1.3.1) isoenzymes. Including wheat germ lectin in the equilibration buffer improved the resolution of the bone and liver isoenzymes. Unlike previously described wheat germ lectin affinity electrophoresis methods, the procedure measures bone, liver, and biliary isoenzymes in a single step. There was good correlation between the affinity electrophoresis and the neuraminidase preincubation methods for the measurement of bone (r = 0.958) and liver (r = 0.962) alkaline phosphatase isoenzymes. However, the affinity electrophoresis method also quantified minor isoenzyme fractions that were poorly resolved by the neuraminidase method. The method is technically simple, reproducible, and capable of rapid handling of large workloads.

Hypophosphatasia (adult form): quantitation of serum alkaline phosphatase isoenzyme activity in a large kindred.

1980 ◽  
Vol 26 (7) ◽  
pp. 840-845 ◽  
Author(s):  
J L Millán ◽  
M P Whyte ◽  
L V Avioli ◽  
W H Fishman
Keyword(s):  
Alkaline Phosphatase ◽  
Serum Alkaline Phosphatase ◽  
Hepatic Metabolism ◽  
Total Activity ◽  
Heat Inactivation ◽  
Mean Values ◽  
Adult Form ◽  
Cellulose Acetate Membranes ◽  
Alkaline Phosphatase Isoenzymes ◽  
Alkaline Phosphatase Isoenzyme

Abstract We used heat inactivation, L-phenylalanine inhibition, and electrophoresis on polyacrylamide gel and cellulose acetate membranes--with and without use of specific antisera against the liver-bone, intestinal, and placental isoenzymes--to distinguish and quantitate the different alkaline phosphatase isoenzymes in sera from 23 adult members of a kindred affected by the adult form of hypophosphatasia. Nine subjects had values for total activity more than two standard deviations below the mean values for age- and sex-matched normal persons. Bone isoenzyme was diminished in all nine, whereas liver isoenzyme was subnormal in only four. Phosphoethanolamine and phosphoserine in the urine of eight hypophosphatasemic individuals correlated inversely with both total and liver alkaline phosphatase activity in their serum, but not with the activity of the bone isoenzyme. Total activity in the serum of adult kindred members correlated best with the circulating liver isoenzyme activity. The findings suggest that altered hepatic metabolism is responsible for the increased urinary excretion of phosphoethanolamine, and perhaps phosphoserine, in hypophosphatasia.

THE RELATIONSHIP OF DIETARY FACTORS TO RAT SERUM ALKALINE PHOSPHATASE: 1. THE EFFECT OF FAT, METHIONINE, AND CYSTINE

1950 ◽  
Vol 28e (2) ◽  
pp. 41-46 ◽  
Author(s):  
Jules Tuba ◽  
Ridley K. Shaw
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Serum Alkaline Phosphatase ◽  
Dietary Factors ◽  
Rat Serum ◽  
Serum Alkaline Phosphatase Activity ◽  
Weight Losses ◽  
Weanling Rats ◽  
Standard Laboratory Diet ◽  
Relationship Of

In synthetic diets fed to weanling rats, methionine and fat must be present in a definite ratio in order to maintain a serum alkaline phosphatase activity equal to that obtained on a standard laboratory diet of animal checkers. This ratio is approximately 1:25 by weight for a diet containing 8.5% fat. Increased fat enhances, while increased methionine lowers, the serum phosphatase activity. Although in some experiments methionine was fed in concentrations sufficient to lower phosphatase activity to what has been considered definitely subnormal values, growth was good and the general condition of the animals was excellent. However, beyond certain concentrations of the amino acid, food consumption decreased and weight losses occurred. Cystine had no effect in opposing the action of methionine on serum alkaline phosphatase.

Characterization of placental isoenzyme of alkaline phosphatase in human pregnancy serum

1969 ◽  
Vol 47 (2) ◽  
pp. 147-155 ◽  
Author(s):  
N. K. Ghosh ◽  
W. H. Fishman
Keyword(s):  
Alkaline Phosphatase ◽  
Serum Alkaline Phosphatase ◽  
Heat Stability ◽  
Biochemical Properties ◽  
Heat Inactivation ◽  
Total Serum ◽  
Placental Alkaline Phosphatase ◽  
Human Placental Alkaline Phosphatase ◽  
Alkaline Phosphatase Isoenzyme ◽  
In Pregnancy

Human placental alkaline phosphatase isoenzyme has been characterized in pregnancy serum by several biochemical criteria. The total serum alkaline phosphatase, its L-phenylalanine-sensitive moiety, heat inactivation, and the ratio of enzyme activity at pH 10.7 versus 9.8 (10.7/9.8 R) were measured during parturition and 59 weeks of pre- and post-natal periods. The extent of L-phenylalanine inhibition, heat stability, and 10.7/9.8 R of serum alkaline phosphatase progressively increased during gestation attaining maximum values during the delivery, after which they gradually declined. The electrophoretic behaviors of alkaline phosphatase isoenzymes of pregnancy sera were followed by starch- and Sephadex-gel electrophoreses. Alkaline phosphatase has been purified 300-fold from the placenta of the subject whose serum enzyme was investigated. The biochemical properties, including the electrophoretic behavior and neuraminidase sensitivity of heat-stable alkaline phosphastase in pregnancy sera at term, were comparable to those of purified placental alkaline phosphatase. The values for 10.7/9.8 R of the pregnancy sera were statistically different from those of sera from normal nonpregnant women. The results obtained in this study suggest that the enhanced level of pregnancy serum alkaline phosphatase is due to the enrichment of the circulation with an isoenzyme of placental origin.

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