Analysis of serum corticosteroid-induced alkaline phosphatase isoenzyme in dogs with hepatobiliary diseases

2017 ◽  
Vol 58 (5) ◽  
pp. 257-262 ◽  
Author(s):  
K. Kojima ◽  
K. Ohno ◽  
H. Kanemoto ◽  
Y. Goto-Koshino ◽  
K. Fukushima ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Hepatobiliary Diseases ◽  
Alkaline Phosphatase Isoenzyme

Quantitative alkaline phosphatase isoenzyme determination by electrophoresis on cellulose acetate membranes.

1977 ◽  
Vol 23 (1) ◽  
pp. 28-34 ◽  
Author(s):  
W H Siede ◽  
U B Seiffert
Keyword(s):  
Alkaline Phosphatase ◽  
Cellulose Acetate ◽  
Clinical Laboratory ◽  
Kinetic Assay ◽  
Specific Staining ◽  
Cellulose Acetate Membranes ◽  
Alkaline Phosphatase Isoenzymes ◽  
Elution Method ◽  
Routine Clinical Laboratory ◽  
Alkaline Phosphatase Isoenzyme

Abstract We present a new method for quantitative determination of alkaline phosphatase isoenzymes. This method consists of electrophoretic separation on cellulose acetate membranes, special fixation technique to avoid elution and diffusion of enzyme protein during incubation, specific staining, and quantitative evaluation by densitometric measurement. We highly recommend the precedure for routine clinical laboratory use. In all normal individuals we observe two isoenzymes of hepatic origin and one isoenzyme each of osseous, intestinal, and biliary origin. Quantitative normal values are presented. Precision of the method is calculated, the CV being less than 10%. The exactness of densitometric quantification is proved by comparison with kinetic assay of alkaline phosphatase isoenzymes by use of an elution method. Clinical implications of alkaline phosphatase isoenzymograms are reported and discussed in detail.

Clinical usefulness of alkaline phosphatase isoenzyme determinations

1977 ◽  
Vol 10 ◽  
pp. 171-174 ◽  
Author(s):  
Linda Gorman ◽  
Bernard E. Statland
Keyword(s):  
Alkaline Phosphatase ◽  
Clinical Usefulness ◽  
Alkaline Phosphatase Isoenzyme

Changes in Serum Succinyltrialanine P-Nitroanilide Hydrolysing Activity in Hepatobiliary Diseases

1979 ◽  
Vol 16 (1-6) ◽  
pp. 320-324 ◽  
Author(s):  
Michio Ogawa ◽  
Kenjiro Iwaki ◽  
Naoko Saito ◽  
Shigenori Tanaka ◽  
Goro Kosaki
Keyword(s):  
Alkaline Phosphatase ◽  
Intrahepatic Cholestasis ◽  
Acute Cholangitis ◽  
Phosphatase Activities ◽  
Hepatobiliary Diseases

Serum succinyltrialanine p-nitroanilide hydrolysing activity was elevated in patients with hepatobiliary diseases. The highest activities were seen in acute cholangitis and intrahepatic cholestasis. The change in succinyltrialanine p-nitroanilide hydrolysing activity was closely associated with those in γ-glutamyltranspeptidase and alkaline phosphatase activities. In some cases, however, the former was more sensitive than the latter.

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.

Detection of Regan Variant Type of Alkaline Phosphatase Isoenzyme in Liver Tissue of Indian Childhood Cirrhosis

Hepatology ◽  
2007 ◽  
Vol 3 (4) ◽  
pp. 572-576
Author(s):  
S. R. Parekh ◽  
B. D. Patel ◽  
S. R. Damle ◽  
G. M. Thanki ◽  
D. Khutti
Keyword(s):  
Alkaline Phosphatase ◽  
Liver Tissue ◽  
Indian Childhood Cirrhosis ◽  
Variant Type ◽  
Indian Childhood ◽  
Alkaline Phosphatase Isoenzyme

Alkaline phosphatase isoenzymes.

1982 ◽  
Vol 28 (10) ◽  
pp. 2007-2016 ◽  
Author(s):  
D W Moss
Keyword(s):  
Alkaline Phosphatase ◽  
Quantitative Analysis ◽  
Posttranslational Modifications ◽  
Quantitative Methods ◽  
Molecular Forms ◽  
Future Research ◽  
Alkaline Phosphatases ◽  
Isoenzyme Analysis ◽  
Alkaline Phosphatase Isoenzymes ◽  
Alkaline Phosphatase Isoenzyme

Abstract The human alkaline phosphatases constitute a system of multiple molecular forms of enzymes in which heterogeneity is partly due to genetic factors and partly to posttranslational modifications. Recognition of the nature and occurrence of these multiple forms has made a significant contribution both to the understanding of changes in alkaline phosphatase values for serum in disease and to the use of alkaline phosphatase measurements in diagnosis. Many of the diagnostic advantages of alkaline phosphatase isoenzyme analysis can be obtained with the aid of qualitative methods such as zone electrophoresis. However, quantitative methods are needed to take full advantage of the potential benefits of isoenzyme analysis. Selective inactivation methods can be applied successfully to the quantitative analysis of bone and liver alkaline phosphatases in serum. However, the aim of future research should be to remove the limitations at present imposed on quantitative analysis by the close similarities of bone and liver alkaline phosphatases.

Use of monoclonal antibodies to detect human placental alkaline phosphatase.

1983 ◽  
Vol 29 (1) ◽  
pp. 115-119 ◽  
Author(s):  
G De Groote ◽  
P De Waele ◽  
A Van de Voorde ◽  
M De Broe ◽  
W Fiers
Keyword(s):  
Monoclonal Antibody ◽  
Alkaline Phosphatase ◽  
Monoclonal Antibodies ◽  
Solid Phase ◽  
Enzymatic Reactions ◽  
Placental Alkaline Phosphatase ◽  
Human Placental Alkaline Phosphatase ◽  
Human Sera ◽  
Starch Gel ◽  
Alkaline Phosphatase Isoenzyme

Abstract Convenient, sensitive, and specific solid-phase immunoassays involving monoclonal antibody are described for the determination of human placental alkaline phosphatase (hPLAP). An endogenous enzyme immunoassay combined the specificity of the immunological and the enzymatic reactions. Alternatively, a solid-phase "sandwich" radioimmunoassay involving immobilized polyclonal rabbit anti-hPLAP in combination with iodinated monoclonal antibody provided some additional advantages. Both tests can be used to detect hPLAP from various sources, e.g., in human sera during pregnancy or as a tumor marker. The radioimmunoassay detected an increase in hPLAP at nine weeks of gestation. We discuss the use of monoclonal antibodies for the differentiation of different alkaline phosphatase isoenzyme types by electrophoresis on starch gel.

An alkaline phosphatase isoenzyme mystery: a challenge to the reader.

1989 ◽  
Vol 35 (4) ◽  
pp. 707-708
Author(s):  
S B Rosalki ◽  
A Y Foo ◽  
A W Johnson
Keyword(s):  
Alkaline Phosphatase ◽  
Alkaline Phosphatase Isoenzyme

A fetal intestinal-type alkaline phosphatase in hepatocellular carcinoma tissue.

1977 ◽  
Vol 23 (9) ◽  
pp. 1615-1623 ◽  
Author(s):  
K Higashino ◽  
R Otani ◽  
S Kudo ◽  
Y Yamamura
Keyword(s):  
Alkaline Phosphatase ◽  
Electrophoretic Mobility ◽  
Normal Liver ◽  
Heat Stability ◽  
Intestinal Type ◽  
Intestinal Alkaline Phosphatase ◽  
Alkaline Phosphatases ◽  
Adult Type ◽  
Alkaline Phosphatase Isoenzyme ◽  
Hepatocellular Carcinoma Tissue

Abstract We examined 19 hepatoma tissues for alkaline phosphatase isoenzyme and found that six have both the Kasahara isoenzyme and an alkaline phosphatase with a unique electrophoretic mobility, in addition to the liver-type enzyme. From two of six carcinoma tissues, the abnormal enzyme was partly purified and subjected to a detailed analysis, which clarified that the abnormal enzyme resembled a fetal intestinal alkaline phosphatase in most of its enzymic and immunologic properties and also in properties that reflect enzyme structure. This fetal intestinal-type alkaline phosphatase was not found in 24 specimens of normal liver from adults. The relevance of fetal intestinal-type alkaline phosphatase to Kasahara isoenzyme and adult intestinal alkaline phosphatase is discussed. The fetal and adult intestinal alkaline phosphatases differ in electrophoretic mobility, heat stability, and reactivity with concanavalin A. The adult-type enzyme has two components; only the electrophoretically slower, neuraminidase-resistant one is described here.

scholarly journals Bone alkaline phosphatase isoenzyme in renal osteodystrophy

1996 ◽  
Vol 11 (supp3) ◽  
pp. 43-46 ◽  
Author(s):  
C. Jarava ◽  
J. R. Armas ◽  
M. Salgueira ◽  
A. Palma
Keyword(s):  
Alkaline Phosphatase ◽  
Renal Osteodystrophy ◽  
Bone Alkaline Phosphatase ◽  
Alkaline Phosphatase Isoenzyme
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