Atypical alkaline phosphatase isoenzyme in serum from a patient with Hodgkin's disease.

1984 ◽  
Vol 30 (5) ◽  
pp. 800-802 ◽  
Author(s):  
J P Beilby ◽  
P Garcia-Webb ◽  
C I Bhagat ◽  
A Prins
Keyword(s):  
Alkaline Phosphatase ◽  
Molecular Mass ◽  
Hodgkin's Disease ◽  
Serum Alkaline Phosphatase ◽  
Hodgkin’S Disease ◽  
Heat Inactivation ◽  
Relative Molecular Mass ◽  
Agarose Gel Electrophoresis ◽  
Post Translational Modification ◽  
Alkaline Phosphatase Isoenzyme

Abstract An alkaline phosphatase isoenzyme that did not move from the origin in agarose gel electrophoresis was detected in serum from a 51-year-old woman with Hodgkin's disease. Inhibitor and heat-inactivation studies of the patient's serum alkaline phosphatase showed properties resembling those of both liver and bone isoenzymes. No immunoglobulin or high-molecular-mass complexes with the alkaline phosphatase isoenzyme were detected. The relative molecular mass (Mr) of the atypical alkaline phosphatase isoenzyme was 182 000, that of the liver alkaline phosphatase isoenzyme control 170 000. Treatment of both of these isoenzymes with neuraminidase gave a product with an Mr of 140 000. We propose that a post-translational modification increased the carbohydrate content of the liver alkaline phosphatase isoenzyme, thus changing the charge characteristics of the enzyme and decreasing its electrophoretic mobility. We believe this to be the first report of a post-translational modification in a heat-sensitive isoenzyme of alkaline phosphatase.

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.

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.

Purification of an alkaline phosphatase-lipoprotein-X complex.

1980 ◽  
Vol 26 (5) ◽  
pp. 604-608 ◽  
Author(s):  
R N Weijers ◽  
H Kruijswijk ◽  
J M Baak
Keyword(s):  
Alkaline Phosphatase ◽  
Affinity Chromatography ◽  
Molecular Mass ◽  
Gel Filtration ◽  
Relative Molecular Mass ◽  
Agarose Gel ◽  
Extrahepatic Cholestasis ◽  
Abnormal Position ◽  
Alkaline Phosphatase Isoenzyme ◽  
Isoenzyme Patterns

Abstract An alkaline phosphatase isoenzyme was observed in an abnormal position in the agar-agarose gel pattern of sera from several patients suffering from intrahepatic and extrahepatic cholestasis. We purified this isoenzyme, by gel filtration and affinity chromatography, from the serum of a patient suffering from extrahepatic cholestasis. Analysis demonstrated an alkaline phosphatase-lipoprotein-X complex with a relative molecular mass of at least 669,000. We discuss the interpretation of alkaline phosphatase isoenzyme patterns produced by different techniques.

Purification of an alkaline phosphatase-lipoprotein-X complex.

1980 ◽  
Vol 26 (5) ◽  
pp. 604-608
Author(s):  
R N Weijers ◽  
H Kruijswijk ◽  
J M Baak
Keyword(s):  
Alkaline Phosphatase ◽  
Affinity Chromatography ◽  
Molecular Mass ◽  
Gel Filtration ◽  
Relative Molecular Mass ◽  
Agarose Gel ◽  
Extrahepatic Cholestasis ◽  
Abnormal Position ◽  
Alkaline Phosphatase Isoenzyme ◽  
Isoenzyme Patterns

Abstract An alkaline phosphatase isoenzyme was observed in an abnormal position in the agar-agarose gel pattern of sera from several patients suffering from intrahepatic and extrahepatic cholestasis. We purified this isoenzyme, by gel filtration and affinity chromatography, from the serum of a patient suffering from extrahepatic cholestasis. Analysis demonstrated an alkaline phosphatase-lipoprotein-X complex with a relative molecular mass of at least 669,000. We discuss the interpretation of alkaline phosphatase isoenzyme patterns produced by different techniques.

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.

scholarly journals Serum alkaline phosphatase at the onset of Hodgkin's disease

Cancer ◽  
1970 ◽  
Vol 26 (2) ◽  
pp. 318-326 ◽  
Author(s):  
Alan C. Aisenberg ◽  
Marshall M. Kaplan ◽  
Sidney V. Rieder ◽  
John M. Goldman
Keyword(s):  
Alkaline Phosphatase ◽  
Hodgkin's Disease ◽  
Serum Alkaline Phosphatase ◽  
Hodgkin’S Disease

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.

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

"Fragmented" isoenzymes of alkaline phosphatase in the diagnosis of transient hyperphosphatasemia.

1986 ◽  
Vol 32 (12) ◽  
pp. 2211-2213 ◽  
Author(s):  
E Schoenau ◽  
K H Herzog ◽  
H J Boehles
Keyword(s):  
Alkaline Phosphatase ◽  
Liquid Chromatography ◽  
Cellulose Acetate ◽  
Serum Alkaline Phosphatase ◽  
Heat Inactivation ◽  
Similar Increase ◽  
Cellulose Acetate Membranes

Abstract We describe the appearance of "fragmented" isoenzymes of serum alkaline phosphatase (EC 3.1.3.1) in two cases of transient hyperphosphatasemia. We determined the isoenzymes by liquid chromatography, then characterized them by heat inactivation, inhibition with 5 mmol/L L-phenylalanine solution, and electrophoresis on cellulose acetate membranes. We suspect that a virus-induced decrease in clearance of the enzyme from serum is responsible for a similar increase of bone and liver isoenzyme activities and for the presence of these fragmented isoenzymes in transient hyperphosphatasemia.

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