Abnormal lactate dehydrogenase isoenzyme in serum and tumor tissue of a patient with neuroblastoma.

1985 ◽  
Vol 31 (2) ◽  
pp. 318-320 ◽  
Author(s):  
N Otsu ◽  
M Hirata ◽  
K Miyazawa ◽  
S Tuboi
Keyword(s):  
Lactate Dehydrogenase ◽  
Gel Electrophoresis ◽  
Tumor Tissue ◽  
Surgical Removal ◽  
Marker Enzyme ◽  
Agarose Gel Electrophoresis ◽  
Neurogenic Tumors ◽  
Ldh Activity ◽  
Ldh Isoenzyme ◽  
Normal Human

Abstract Serum and tumor tissue of a patient with neuroblastoma contained an abnormal isoenzyme of lactate dehydrogenase (LDH; EC 1.1.1.27), which, on agarose gel electrophoresis, migrated between LDH-2 and LDH-3 with a mobility the same as that of the extra LDH isoenzyme found in normal human erythrocytes. On surgical removal of the tumor, the high total LDH activity (775 U/L) in the serum of the patient rapidly decreased to normal (70-220 U/L), and the abnormal LDH isoenzyme was no longer detected. The total LDH activity of the abnormal LDH isoenzyme per gram of hemoglobin in the tumor tissue was 26 times that of erythrocytes, suggesting that the abnormal isoenzyme originated mainly from the tumor cells themselves rather than the erythrocytes contained in the tumor tissue. This first report on the appearance of the abnormal LDH isoenzyme in a patient with neuroblastoma suggests that this abnormal LDH isoenzyme may have some significance as a marker enzyme for neurogenic tumors.

scholarly journals The determination of lactate dehydrogenase isoenzymes in normal human muscle and other tissues

1967 ◽  
Vol 105 (2) ◽  
pp. 599-604 ◽  
Author(s):  
A. E. H. Emery
Keyword(s):  
Lactate Dehydrogenase ◽  
Gel Electrophoresis ◽  
Human Muscle ◽  
Starch Gel Electrophoresis ◽  
Fibrous Connective Tissue ◽  
Starch Gel ◽  
Normal Human ◽  
Lactate Dehydrogenase Isoenzymes ◽  
Good Agreement

1. A technique has been developed, based on preferential inhibition by urea, for determining the amounts and proportions of the M and H sub-units of lactate dehydrogenase (referred to as LDH-M and LDH-H respectively) in human tissues, including muscle. 2. There was good agreement between the results obtained with urea inhibition and those obtained with starch-gel electrophoresis. 3. With increasing age there was a significant decrease in the total amount of lactate dehydrogenase and the amount of LDH-M in skeletal muscle. This could not be accounted for by the replacement of functioning muscle tissue by fibrous connective tissue. 4. The proportion of LDH-M was less in certain muscles (e.g. soleus and extra-ocular) than in other muscles (e.g. gastrocnemius and rectus abdominis). 5. The proportions of LDH-M and LDH-H did not differ significantly in different superficial limb muscles and were not significantly affected by either age or sex. 6. Specimens of muscle from 86 different individuals (all Europeans) have been subjected to electrophoresis, but no variants of lactate dehydrogenase isoenzymes have been found.

Lactate dehydrogenase isoenzyme pattern in sera of patients with malignant diseases.

1989 ◽  
Vol 35 (3) ◽  
pp. 396-399 ◽  
Author(s):  
E E Giannoulaki ◽  
D L Kalpaxis ◽  
C Tentas ◽  
P Fessas
Keyword(s):  
Lactate Dehydrogenase ◽  
Heat Stability ◽  
Surgical Removal ◽  
Anatomical Location ◽  
Malignant Diseases ◽  
Serum Samples ◽  
Ldh Isoenzymes ◽  
Ldh Activity ◽  
The Relationship ◽  
Isoenzyme Patterns

Abstract Total lactate dehydrogenase (LDH; EC 1.1.1.27) activity and the percentage distribution of LDH isoenzymes were determined in 127 patients with malignant diseases. A shift in the isoenzyme patterns was observed toward the M-type, with an increase in the percentage of LDH-4 and LDH-5 isoenzymes and a slight increase in total LDH activity of all patients. Serum samples from 68 of the patients contained an abnormal isoenzyme of LDH, "LDH-1 ex," that, on agarose gel electrophoresis at pH 8.6, migrated between albumin and LDH-1 isoenzyme. Chemotherapy, radiotherapy, or surgical removal of the tumor was accompanied by disappearance of this abnormal isoenzyme. The heat stability of LDH-1 ex isoenzyme appears to be similar to that of LDH-1 but greater than that of the other LDH isoenzymes. Statistical analysis of these data demonstrated a significant correlation between malignancy and the appearance of LDH-1 ex isoenzyme (P less than 0.001). In contrast, the relationship between LDH-1 ex isoenzyme and metastasis or anatomical location of the malignancy is not statistically important (P less than 0.1).

Association of an oxygen-sensitive lactate dehydrogenase isoenzyme, LDk, with LD-6 in serum of critically ill patients.

1984 ◽  
Vol 30 (10) ◽  
pp. 1603-1606 ◽  
Author(s):  
V A Onorato ◽  
K F Manly ◽  
A O Vladutiu
Keyword(s):  
Lactate Dehydrogenase ◽  
Critically Ill ◽  
Critically Ill Patients ◽  
Gel Electrophoresis ◽  
Malignant Tumors ◽  
High Serum ◽  
Agarose Gel Electrophoresis ◽  
Severe Hypotension ◽  
Oxygen Sensitive ◽  
Very High

Abstract We measured a highly unusual, oxygen-sensitive lactate dehydrogenase, LDk, in the serum of six patients whose serum showed a band for LD-6 on routine agarose gel electrophoresis for LD isoenzymes. All these patients showed very high serum LDk activity, greatly exceeding the high values previously described in serum of patients with various malignant tumors. In two of the patients, LDk activity was low both before LD-6 was found in and after it disappeared from the serum, evidencing a correlation with LD-6. All of the six patients, five of whom died in the hospital, had severe hypotension. We suggest that hypoxia is responsible for the appearance of LD-6 in serum and that LD-6 is found in association with high LDk activity in serum of critically ill patients.

Tissue specific isozymes of alanopine dehydrogenase in the channeled whelk Busycotypus canaliculatum

1982 ◽  
Vol 60 (7) ◽  
pp. 1568-1572 ◽  
Author(s):  
William C. Plaxton ◽  
Kenneth B. Storey
Keyword(s):  
Lactate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Physiological Functions ◽  
Ldh Activity ◽  
Muscle Tissues ◽  
Proboscis Muscles ◽  
Octopine Dehydrogenase ◽  
Muscular Tissues

The tissues of the channeled whelk Busycotypus canaliculatum displayed activities of three glycolytic dehydrogenases, alanopine dehydrogenase (ADH), octopine dehydrogenase (ODH), and lactate dehydrogenase (LDH). ADH and ODH were present in all seven tissues (hepatopancreas, gill, kidney, and mantle, ventricle, foot, and proboscis muscles) tested. ADH was the major cytosolic dehydrogenase activity in all tissues except proboscis, while ODH was present in high activities only in the four muscular tissues. Significant LDH activity occurred only in the two muscles which perform sustained work, ventricle, and proboscis.Tissue specific isozymes of ADH were identified. Three forms, specific for hepatopancreas, gill–kidney, and muscle tissues, were separable by isoelectrofocusing (pI's 5.69, 5.58, and 5.93, respectively), chromatofocusing, and polyacrylamide gel electrophoresis. The three isozymes differed kinetically showing significant differences in apparent Km's for L-alanine (e.g., 8.84 ± 0.03, 10.64 ± 0.40, and 13.12 ± 0.65 mM for hepatopancreas, ventricle, and gill, respectively) and even greater differences in apparent Km's for glycine (619 ± 55, 1412 ± 115, and 2542 ± 230 mM for the above three tissues, respectively). The ratios Km(gly)/Km(ala) averaged 70, 192, and 132 for the three isozymes, hepatopancreas, gill–kidney and muscle, respectively.The physiological functions of ADH isozymes in the whelk may be similar to those of the M and H isozymes of LDH in vertebrates or the muscle and brain specific isozymes of ODH in cephalopod molluscs.

Lactate dehydrogenase in human maxillary adenocarcinoma and in experimental adenocarcinoma in mice

1985 ◽  
Vol 99 (2) ◽  
pp. 171-175 ◽  
Author(s):  
Wiesław Gołabek ◽  
Leonard M. Franks
Keyword(s):  
Lactate Dehydrogenase ◽  
Lung Adenocarcinoma ◽  
Lung Tissue ◽  
Isoenzyme Pattern ◽  
Normal Lung Tissue ◽  
Normal Lung ◽  
Ldh Activity ◽  
Ldh Isoenzyme ◽  
Human Tumours

Total lactate dehydrogenase (LDH) activity and isoenzyme pattern were studied in tumore tissue from eight patients with maxillary adenocarcinoma, chronic inflammatory mucosa from 12 patients, normal maxillary mucosa from 12 patients, and an experimental lung adenocarcinoma and normal lung tissue from 12 mice.An increase in the total LDH activity and cathodic shift in LDH isoenzyme pattern was found in human maxillary adenocarcinoma as compared to normal and inflammatory mucosa. The inflammatory mucosa showed an increase in the total LDH activity and a normal isoenzyme pattern. The LDH alterations in the total LDH activity and a normal isoenzyme pattern. The LDH alterations in the experimental lung adenocarcinoma in mice were similar to those in the human tumours but they were much more marked.

Isozymic pattern of lactate dehydrogenase in cases of bancroftian filariasis

1992 ◽  
Vol 66 (2) ◽  
pp. 142-146
Author(s):  
S. Misra ◽  
T. M. Mahopatra ◽  
S. Rathaur
Keyword(s):  
Lactate Dehydrogenase ◽  
Gel Electrophoresis ◽  
Healthy Subjects ◽  
Polyacrylamide Gel Electrophoresis ◽  
Combined Treatment ◽  
Gel Filtration ◽  
Bancroftian Filariasis ◽  
Ldh Activity ◽  
Isozymic Pattern ◽  
Endemic Normal

ABSTRACTIsozymic patterns of lactate dehydrogenase (E.C. 1.1.1.27) by polyacrylamide gel electrophoresis (PAGE) were observed m various categories of filariasis and controls, i.e. asymptomatic microfilaraemia and symptomatic amicrofilaraemia, endemic normal and non-endemic normal. Lactate dehydrogenase (LDH) activity was also observed amongst the above categories of patients. An increase in enzyme activity and change in the isozymic pattern was observed in the above categories of filaria infected serum. LDH activity doubled in asymptomatic microfilaraemia whereas in symptomatic amicrofilaraemia the increase in LDH activity was thirtyfold. The isozymic pattern of microfilaraemia cases showed the presence of three bands B4, A1B3, A2 B2, which are quite thick as compared to normal healthy subjects, whereas the patients with symptomatic amicrofilaraemia showed marked elevation of serum LDH-4 or A3B1. The LDH was partially purified by combined treatment of (NH4)2SO4 fractionation and gel filtration. The isozymic pattern of purified LDH showed a similar pattern.

scholarly journals Color developmental conditions for LDH isoenzyme assay by agarose gel electrophoresis.

1985 ◽  
Vol 29 (6) ◽  
pp. 403-406
Author(s):  
Itsuo Kuroda ◽  
Chinami Nakazawa ◽  
Kohsuke Mori ◽  
Mitsutaka Yoshida
Keyword(s):  
Gel Electrophoresis ◽  
Agarose Gel ◽  
Agarose Gel Electrophoresis ◽  
Ldh Isoenzyme ◽  
Developmental Conditions

Electrophoresis and the isomune-LD and LD-1 immuno methods compared for measurement of lactate dehydrogenase isoenzyme-1.

1987 ◽  
Vol 33 (10) ◽  
pp. 1884-1886
Author(s):  
P Ranjan ◽  
R E Karcher ◽  
E Epstein ◽  
F L Kiechle
Keyword(s):  
Lactate Dehydrogenase ◽  
Gel Electrophoresis ◽  
Agarose Gel ◽  
Agarose Gel Electrophoresis ◽  
Regression Analyses ◽  
Mean Values ◽  
Creatine Kinase Mb ◽  
Significant Difference ◽  
The Mean ◽  
Paired T Test

Abstract We evaluated three different methods for measuring lactate dehydrogenase (EC 1.1.1.27) isoenzyme LD-1 activity--agarose gel electrophoresis and two immunoassays, Isomune-LD (Roche) and LD-1 Immuno (Seragen)--in patients' samples for which measurement of creatine kinase-MB was ordered. Regression analyses of the comparisons gave the following results: LD-1 (%) from Isomune-LD (y) vs electrophoresis (x) (n = 51), y = 1.05x + 1.99, r = 0.92; LD-1 (%) from LD-1 Immuno (y) vs electrophoresis (n = 27), y = 1.05x + 3.94, r = 0.88; LD-1 (%) from LD-1 Immuno (y) vs Isomune-LD (x) (n = 41), y = 1.06x + 0.48, r = 0.95. Comparison by Student's paired t-test yielded significant differences between the mean values by electrophoresis and both Isomune-LD (P less than 0.005) and LD-1 Immuno (P less than 0.001), but no significant difference between the two immunoassays (P greater than 0.2). Analyzing these results by the overlap index, we conclude that electrophoresis shows the best clinical correlation followed, in order, by the Isomune-LD and the LD-1 Immuno methods. Both immunoassays are simpler and more rapid than electrophoresis, but in our hands the Isomune-LD method demonstrated greater precision and better correlation with electrophoretic values.

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