The gamma-glutamyltransferase isoenzyme pattern in serum as a signal discriminating between hepatobiliary diseases, including neoplasias.

1988 ◽  
Vol 34 (2) ◽  
pp. 352-355 ◽  
Author(s):  
L Sacchetti ◽  
G Castaldo ◽  
F Salvatore
Keyword(s):  
Normal Subjects ◽  
Isoenzyme Pattern ◽  
Specific Marker ◽  
Hepatic Tumors ◽  
Diagnostic Specificity ◽  
Reference Pattern ◽  
Gamma Glutamyltransferase ◽  
Hepatobiliary Diseases ◽  
Electrophoretic Procedure ◽  
Metastatic Liver

Abstract We have used the gamma-glutamyltransferase (GGT) isoenzyme pattern in serum as a means for discriminating between hepatobiliary diseases, including neoplasias. The reference pattern, determined in 142 normal subjects with a simplified conventional cellulose acetate electrophoretic procedure, contained two GGT bands, alpha 1-GGT and alpha 2-GGT, in proportions of 60-80% and 20-40%, respectively. Sera from 95 hepatobiliary patients showed typical isoenzyme features: (a) a beta-migrating GGT form that was less than 10% of the total GGT in chronic hepatitis and cirrhosis, and less than or equal to 30% of the total GGT in cirrhosis with intrahepatic cholestasis and in cases of extra- and intrahepatic obstructive jaundice, including liver neoplasias; (b) a gamma-migrating GGT band and (or) a "dep-GGT" (nonmigrating) band in cases of extrahepatic jaundice; and (c) an albumin-migrating GGT band that had a diagnostic sensitivity of 75% for hepatic tumors. The diagnostic specificity of this last band is 92% toward other hepatic disorders and 91% toward nonhepatic neoplasias; we consider it a potential specific marker for primary or metastatic liver neoplasias.

Improved procedure for measuring gamma-glutamyltransferase isoenzymes in serum.

1988 ◽  
Vol 34 (2) ◽  
pp. 419-422 ◽  
Author(s):  
L Sacchetti ◽  
G Castaldo ◽  
G Fortunato ◽  
F Salvatore
Keyword(s):  
Scattered Light ◽  
Density Lipoprotein ◽  
Normal Subjects ◽  
Total Activity ◽  
Coumarin Derivative ◽  
Very Low Density Lipoproteins ◽  
Gamma Glutamyltransferase ◽  
Analytical Imprecision ◽  
Hepatobiliary Diseases ◽  
Electrophoretic Procedure

Abstract In this electrophoretic procedure for measuring isoenzymes of gamma-glutamyltransferase, patterns obtained are highly reproducible and the analytical imprecision (CV) ranges from 1.10% to 6.17%. A cellulose acetate support is used, at 220 V for 40 min. Sharply resolved isoenzyme bands were made visible by fluorescence scattered light, formed by use of a coumarin derivative as donor substrate. Two bands were observed for sera from normal subjects; four bands were variably present in sera from patients with different hepatobiliary diseases. Detection of the latter was satisfactory, down to a total activity in serum of 8-10 U/L. Three of the pathological bands were associated with low- and (or) very-low-density lipoproteins, whereas a major fraction of one of the normal bands in cirrhotic sera precipitated with high-density lipoprotein. The bands in normal sera, and one of the abnormal bands, did not.

Immunoassay in Urine of a Specific Marker for Proximal Tubular S3 Segment

1992 ◽  
Vol 38 (5) ◽  
pp. 642-647 ◽  
Author(s):  
G F Verpooten ◽  
G D Nuyts ◽  
M F Hoylaerts ◽  
E J Nouwen ◽  
Z Vassanyiova ◽  
...  
Keyword(s):  
Precise Measurement ◽  
Sandwich Elisa ◽  
Human Kidney ◽  
Normal Subjects ◽  
Specific Marker ◽  
Healthy Individuals ◽  
Intestinal Alkaline Phosphatase ◽  
Analytical Recovery ◽  
Proximal Tubular ◽  
S3 Segment

Abstract Urinary intestinal alkaline phosphatase (EC 3.1.3.1; IAP) is a marker of the S3 segment of the human kidney proximal tubule. An accurate enzyme-antigen immunoassay (EAIA) with a high-affinity specific monoclonal antibody (IAP250) developed for this marker has a detection limit below the lowest IAP activity found in urine samples of normal subjects. The intra- and interassay CVs were less than 5%. Mean analytical recovery of pure IAP added to urine was 102% (SD 6%), and the EAIA results correlated well with immunoreactivity (measured by a sandwich ELISA), suggesting that the EAIA detected all of the IAP in urine. In healthy individuals (ages 20-80 years) the IAP concentrations, expressed as urinary creatinine ratios, ranged from 0.1 to 2.0 U/g (5-95 percentiles) without major differences related to sex and age. Workers exposed to mercury, which affects the S3 segment, showed an increased IAP elimination; abusers of analgesics, which affect more distal parts of the nephron, did not. As opposed to currently measured markers, the EAIA offers easy, accurate, and precise measurement of early alterations in the S3 segment.

Associations between serum gamma-glutamyltransferase and apolipoproteins: relationships with hepatobiliary diseases.

1984 ◽  
Vol 30 (8) ◽  
pp. 1318-1321 ◽  
Author(s):  
Y Artur ◽  
M Wellman-Bednawska ◽  
A Jacquier ◽  
G Siest
Keyword(s):  
Total Cholesterol ◽  
Apolipoprotein B ◽  
Limited Proteolysis ◽  
Serum Enzyme ◽  
Gamma Glutamyltransferase ◽  
Apolipoprotein A ◽  
Heavy Form ◽  
Membrane Bound ◽  
Hepatobiliary Diseases ◽  
Light Form

Abstract We studied the association between gamma-glutamyltransferase (GGT) and apolipoproteins A or B in serum of 42 patients with various hepatobiliary diseases. Binding of the enzyme to apolipoprotein A is not related to a clearly defined disease, but appears to be mainly influenced by the ratio of total cholesterol to GGT activity. An important fraction of GGT activity is associated with apolipoprotein B in patients with icteric or anicteric cholestasis. Conversely, in noncholestatic patients, the percentage of apolipoprotein B-bound GGT activity is low. Addition of the "heavy" form of GGT, obtained by solubilizing the membrane-bound enzyme with detergents, to a serum with low GGT activity led to the binding of the enzyme only to apolipoprotein A. The "light" form of GGT, obtained by limited proteolysis of the "heavy" form and added to the same serum, did not bind to either apolipoprotein A or apolipoprotein B. Thus, the association between the serum enzyme and apolipoprotein A apparently results from nonspecific aggregation of the amphiphilic "heavy" form of the enzyme. The origin of the apolipoprotein B-GGT complexes found in cholestatic patients needs further investigation.

scholarly journals Quantitative Abnormalities of Aα Chain Molecular Weight in the Fibrinogen of Cirrhotic Patients

1977 ◽  
Author(s):  
Mark Weinstein ◽  
Daniel Deykin
Keyword(s):  
Molecular Weight ◽  
Plasma Proteins ◽  
Normal Subjects ◽  
Small Samples ◽  
Two Stage ◽  
Large Pore ◽  
Total Range ◽  
Cirrhotic Patients ◽  
Electrophoretic Procedure ◽  
Molecular Weight Heterogeneity

A novel two-stage SDS gel electrophoretic procedure was devised to examine the molecular weight heterogeneity of fibrinogen in small samples of whole plasma from 12 normal and 7 cirrhotic individuals. Fibrinogen was first separated from other plasma proteins on a large pore gel, cut out of the gel, reduced, and separated into its component Aα, Bβ, and γ chains on a second gel. Two major mol wt species—fibrinogen I and II—were observed on the first gel. The ~ 25000 mol wt difference between these two forms reflected a decrease primarily in the size of one of the fibrinogen II Aα chains. In both normals and cirrhotic patients fibrinogen II comprised 30% of the total (range 20–35%). Fibrinogen I and II each contained two major high mol wt Aα chains—Aα/1 and a smaller Aα/2—that differ by 3000 mol wt. In normal fibrinogen I, Aα/2 comprised 33% of the total Aα chains (range 27–41%). In contrast the fibrinogen I of 6 out of the 7 patients had a lower per cent of Aα/2 (range 10–25%). Similar quantitative differences were seen in the decreased fraction of Aα/2 in the fibrinogen II of cirrhotic patients compared to normals. No correlation was found between per cent fibrinogen II and per cent Aα/2 in either normal subjects or cirrhotics. These results suggest that at least two independent processes are responsible for the observed levels of Aα chain heterogeneity in normals and cirrhotics and that one of these processes yields a lower than normal fraction of Aa/2 chains in the fibrinogen of cirrhotic individuals.

scholarly journals Study on heterogeneity of serum γ-glutamyltranspeptidase in normal subjects and patients with hepatobiliary diseases

1977 ◽  
Vol 21 (3) ◽  
pp. 233-239
Author(s):  
Seijin Hosaki ◽  
Kiyoko Sano ◽  
Hiroko Cho ◽  
Junko Manaka
Keyword(s):  
Normal Subjects ◽  
Hepatobiliary Diseases

Unusual gamma-glutamyltransferase isoenzyme pattern in serum in cystic fibrosis.

1985 ◽  
Vol 31 (5) ◽  
pp. 779-779 ◽  
Author(s):  
S B Rosalki ◽  
A Y Foo ◽  
M Hjelm ◽  
R Dinwiddie
Keyword(s):  
Cystic Fibrosis ◽  
Isoenzyme Pattern ◽  
Gamma Glutamyltransferase

Complexes of serum gamma-glutamyltransferase with apolipoproteins and immunoglobulin A.

1984 ◽  
Vol 30 (5) ◽  
pp. 631-633 ◽  
Author(s):  
Y Artur ◽  
M Wellman-Bednawska ◽  
A Jacquier ◽  
G Siest
Keyword(s):  
Enzyme Activity ◽  
Apolipoprotein B ◽  
Immunoglobulin A ◽  
Enzymic Activity ◽  
Healthy Individuals ◽  
Gamma Glutamyltransferase ◽  
Apolipoprotein A ◽  
Hepatobiliary Diseases ◽  
Fraction Bound

Abstract We have detected complexes between gamma-glutamyltransferase and apolipoproteins or immunoglobulin A in sera from patients with hepatobiliary diseases but not in sera from healthy individuals. An average of 52.4% of the enzymic activity was precipitated by antiserum against apolipoprotein A, 29.9% by antiserum against apolipoprotein B, and 9.7% by antiserum against immunoglobulin A. Fifty to 60% of the enzyme activity was inhibited in the immunoprecipitates from the transferase fraction bound to apolipoprotein A or immunoglobulin A, and 21% in the fraction bound to apolipoprotein B. We identified the complexed transferase fractions by electrophoresis.

Serum Adenosine Deaminase: Isoenzymes and Diagnostic Application

1992 ◽  
Vol 38 (7) ◽  
pp. 1322-1326 ◽  
Author(s):  
J P Ungerer ◽  
H M Oosthuizen ◽  
S H Bissbort ◽  
W J Vermaak
Keyword(s):  
Rheumatoid Arthritis ◽  
Acute Lymphoblastic Leukemia ◽  
Adenosine Deaminase ◽  
Infectious Mononucleosis ◽  
Lymphoblastic Leukemia ◽  
Normal Subjects ◽  
Isoenzyme Pattern ◽  
Diagnostic Application ◽  
Macrophage Activity ◽  
Electrophoretic Technique

Abstract Human adenosine deaminase (ADA; EC 3.5.4.4) consists of three isoenzymes: ADA1, ADA1+CP, and ADA2. We developed an electrophoretic technique to distinguish between these three isoenzymes. The isoenzyme pattern was studied in tissue and cell homogenates, as well as in serum from normal subjects and from patients with increased serum ADA who had either hepatitis, infectious mononucleosis, tuberculosis, pneumonia, rheumatoid arthritis, or acute lymphoblastic leukemia (ALL). The highest ADA activity was found in lymphocytes and monocytes. ADA2 could be detected only in monocytes (18% of total ADA activity). It was also the predominant isoenzyme in the sera of controls and all disease groups, except for ALL--the only condition evaluated that is not of an inflammatory nature. We conclude that serum ADA reflects monocyte/macrophage activity or turnover in most diseases studied. The exception is ALL, where serum ADA most probably originates from lymphocyte precursors.

Gamma-glutamyltransferase isoenzyme pattern in workers exposed to tetrachloroethylene

1992 ◽  
Vol 21 (5) ◽  
pp. 661-671 ◽  
Author(s):  
Piero Gennari ◽  
Massimo Naldi ◽  
Roberto Motta ◽  
Maria C. Nucci ◽  
Carmen Giacomini ◽  
...  
Keyword(s):  
Isoenzyme Pattern ◽  
Gamma Glutamyltransferase

Serum Lactate Dehydrogenase Isoenzyme Pattern in non-Hodgkin's lymphomas

1988 ◽  
Vol 3 (4) ◽  
pp. 237-242 ◽  
Author(s):  
B.M. Ricerca ◽  
S. Storti ◽  
S. Campisi ◽  
L. Pagano ◽  
F. Dalla Torre ◽  
...  
Keyword(s):  
Lactate Dehydrogenase ◽  
Normal Subjects ◽  
Serum Lactate ◽  
The Other ◽  
Isoenzyme Pattern ◽  
Serum Lactate Dehydrogenase ◽  
Low Grade ◽  
Significant Difference ◽  
Grade Malignancy ◽  
Hodgkin's Lymphomas

Serum lactate dehydrogenase (S-LDH) and its isoenzyme pattern were assayed in 63 non-Hodgkin's lymphoma (NHL) patients, 37 at diagnosis, 15 at relapse and 11 in complete remission (CR). S-LDH in NHL patients with active disease was higher than in normal subjects and CR patients (p<0.001). Among the isoenzymes, LDH-2 and LDH-5 showed no remarked differences; LDH-1 was reduced and LDH-3 and LDH-4 raised in comparison to the normal group (p<0.001). S-LDH levels and isoenzymes 1 and 4 were influenced by the stage, the histological subgroup and by the presence of general symptoms. In fact, cases in stage IV, with “high-grade malignancy” and with general symptoms, had higher S-LDH levels and more evident LDH-1 and LDH-4 changes than the other stages, the other histopathological subgroups and the cases classified as “A”. S-LDH was the same as in normal subjects in the “low-grade” and “intermediate-grade” malignancies as was LDH-1 in stage II and LDH-4 in stages II and III, in “low-grade” malignancy and in the A cases. In contrast, LDH-3 was always high, with no significant difference in relation to the variables considered. Thus, in NHL, LDH-3 seems to be a reliable marker of the presence of the disease in any case, whereas S-LDH is more related to the spread of the lymphoma.

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