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).

Lactate Dehydrogenase Activity and Isoenzyme Patterns in Serous Middle Ear Effusions

1973 ◽  
Vol 82 (2) ◽  
pp. 192-195 ◽  
Author(s):  
S. K. Juhn ◽  
John S. Huff ◽  
Michael M. Paparella
Keyword(s):  
Lactate Dehydrogenase ◽  
Otitis Media ◽  
Middle Ear ◽  
Biochemical Characterization ◽  
Middle Ear Mucosa ◽  
Lactate Dehydrogenase Activity ◽  
Intracellular Enzyme ◽  
Ldh Activity ◽  
Serous Otitis Media ◽  
Isoenzyme Patterns

Biochemical characteristics of middle ear effusions (MEE) should provide a better understanding of the etiopathogenesis of serous otitis media. In order to develop another parameter for the biochemical characterization of the MEE, lactate dehydrogenase (LDH) and LDH isoenzyme patterns in the serous middle ear effusion and serum from 20 patients with serous otitis media were compared. The LDH activity was measured by the usual spectrophotometric method. The isoenzyme patterns were compared on electropherograms using cellulose polyacetate strips. The LDH activity in MEE was significantly higher (P < 0.001) than it was in serum. Fractions of isoenzymes 1 and 2 were each smaller in MEE than in serum. Isoenzymes 4 and 5 have a significantly higher (P < 0.001) fraction in MEE than in serum. Since LDH is an intracellular enzyme and middle ear mucosa is reported to have high content of isoenzymes 4 and 5, the inflammatory changes in the middle ear mucosa which may release intracellular LDH, are suggested as the cause of both higher activity of LDH and the higher fractions of isoenzymes 4 and 5 in MEE than those in the serum.

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.

Optimum Reaction Conditions for Human Lactate Dehydrogenase Isoenzymes as They Affect Total Lactate Dehydrogenase Activity

1968 ◽  
Vol 14 (8) ◽  
pp. 740-753 ◽  
Author(s):  
Royal J Gay ◽  
Robert B McComb ◽  
George N Bowers
Keyword(s):  
Lactate Dehydrogenase ◽  
Comparative Study ◽  
Substrate Concentration ◽  
Spectrophotometric Assay ◽  
Serum Samples ◽  
Reaction Conditions ◽  
Lactate Dehydrogenase Activity ◽  
Ldh Isoenzymes ◽  
Optimum Reaction ◽  
Lactate Dehydrogenase Isoenzymes

Abstract Optimum reaction conditions at 30° ± 0.5° for two continuous spectrophotometric assay procedures, lactate to pyruvate (L → P) and pyruvate to lactate (P → L), were determined with respect to pH at 30° (pH30) substrate concentration, and coenzyme concentration for the human LDH isoenzymes. For the P → L procedure, broad pH30 optima were within the range of 7.20-7.40 for all the LDH isoenzymes. The coenzyme optima were identical for all of the isoenzymes tested at a reduced NAD concentration of 1.5 x 10-4 M. Pyruvate substrate optima ranged from 7.5 x 10-4 M for LDH1 to 1.7 x 10-3 M for LDH5 at pH30 7.30. For the L → P procedure, the pH30 optima were within the range of 8.30-8.88 for the LDH5 through LDH1 isoenzymes, respectively. Optimum activity was obtained at a NAD concentration of 6.0 x 10-3 M and remained constant at least to 1.8 x 10-2 M for each of the isoenzymes tested. L-Lactate substrate optima ranged from 4.0 x 10-2 M for LDH1 to at least 7.2 x 10-2 M for LDH5. From the isoenzyme studies, the degree of variation possibly involved in either method due to variations in isoenzyme distribution was calculated for total LDH samples. These calculations showed that both methods, P → L and L → P, were essentially equivalent. This equivalency was verified by a comparative study of the two methods on human serum samples.

Alterations in lactate dehydrogenase isoenzyme patterns after therapy with streptokinase or streptococcal infection.

1989 ◽  
Vol 35 (8) ◽  
pp. 1763-1766 ◽  
Author(s):  
S J Podlasek ◽  
D R Dufour ◽  
R A McPherson
Keyword(s):  
Lactate Dehydrogenase ◽  
Serum Samples ◽  
Isoenzyme Analysis ◽  
Intravenous Streptokinase ◽  
Pneumococcal Sepsis ◽  
Streptokinase Therapy ◽  
Streptokinase Infusion ◽  
Isoenzyme Patterns ◽  
Gram Positive Cocci

Abstract Serum samples from patients receiving intravenous streptokinase were examined for evidence of interaction in vivo between streptokinase and lactate dehydrogenase (EC 1.1.1.27; LD). We found that this treatment produced a band of LD activity that remained at the electrophoretic origin of LD isoenzyme analysis. Treatment with tissue plasminogen activator produced no such band. The streptokinase-LD complex could be removed from serum by ultracentrifugation. It remained in the circulation for as long as 48 h after streptokinase infusion. A similar phenomenon was observed in a case of pneumococcal sepsis. Examination of supernates from both cultures of several species of Gram-positive cocci revealed interactions between human LD and Streptococcus groups A and C and also Streptococcus pneumoniae. Evidently streptokinase can form complexes with LD in vivo after either streptokinase therapy or infection, with consequent alteration of the LD isoenzyme pattern.

scholarly journals Lactate dehydrogenase isoenzymes in dental pulp of rats according to stage of root development

2003 ◽  
Vol 14 (1) ◽  
pp. 5-11 ◽  
Author(s):  
Estela Maris Losso ◽  
José Nicolau
Keyword(s):  
Lactate Dehydrogenase ◽  
Root Development ◽  
Dental Pulp ◽  
Female Rat ◽  
Second Molar ◽  
Ldh Isoenzymes ◽  
Stage Of Development ◽  
Ldh Activity ◽  
Electrophoretic Profile ◽  
Molar Teeth

The objective of this study was to present a classification of the root development stage of female rat molar teeth and to evaluate the variation in the lactate dehydrogenase (LDH) activity and electrophoretic isoenzyme profile according to the stage of root development of the molar teeth. We also studied the LDH activity and isoenzymes of the pulp of incisor teeth. The stage of development of the rat first molar at the age of 15 days and that of the second molar at the age of 18 days was classified as the beginning of root formation. At the age of 15 days, the electrophoretic profile of the isoenzymes for the first molar showed a prevalence of LDH-1 followed by LDH-2. However, for the maxillary second molar there was a prevalence of LDH-4 followed by LDH-1, while for the mandibular second molar LDH-1 predominated followed by LDH-2 and LDH-4. From 18 days of age, the prevalence was always of LDH-1. The electrophoretic profile of LDH isoenzymes from the pulp of the incisor teeth at the ages studied (25 and 60 days) showed the following order of prevalence: LDH-1 > LDH-2 > LDH-3 > LDH-4 > LDH-5. These results suggest that there are variations in the prevalence of the various forms of LDH isoenzymes in the dental pulp of rats according to the developmental stage of the root.

scholarly journals Observation on the Changes in Lactate Dehydrogenase Isoenzymes in Post-Burn Patients: Significance in Relation to Creatine Kinase

2009 ◽  
Vol 28 (1) ◽  
pp. 16-21 ◽  
Author(s):  
Riaz Ahmad ◽  
Saba Qayyum ◽  
Absar-ul Hasnain ◽  
Anjum Ara ◽  
Arshad Khan ◽  
...  
Keyword(s):  
Wound Healing ◽  
Creatine Kinase ◽  
Lactate Dehydrogenase ◽  
Quantitative Assessment ◽  
Polyacrylamide Gel Electrophoresis ◽  
Burn Patients ◽  
Burn Wound ◽  
Ldh Isoenzymes ◽  
Ldh Activity ◽  
Lactate Dehydrogenase Isoenzymes

Observation on the Changes in Lactate Dehydrogenase Isoenzymes in Post-Burn Patients: Significance in Relation to Creatine Kinase The present study deals with the quantitative assessment of lactate dehydrogenase isoenzymes in the sera of burn subjects. Efforts are also made here to show better predictive marker value of sera LDH, as a few other known protein markers like creatine kinase and myoglobin have limited analytical value in the management of thermal burns. Blood was initially collected at day-1 of admission from 29 burn and 10 healthy subjects. Further, the sampling was carried out at 2, 5, 10, 20 and 30 days of wound healing (recovery). Plasma and sera LDH isoenzymes were monitored on 7.5% polyacrylamide gel electrophoresis. Quantitative assessment of LDH isoenzymes was done from gelscans using GelPro and Scion Imaging softwares. Sera CK levels were estimated colorimetrically using reagent kits. Our results show that quantitative changes in LDH isoenzyme were more convincing and interpretable in the sera than plasma. Sera LDH-5 isoenzyme was detected as the major contributor of total sera LDH activity, which follows a change parallel to sera CK in burn subjects. Sera LDH-5 activity also remains significantly high for up to 10 days while sera CK levels were detected elevated up to 5 days (P<0.05) during the recovery of patients. Therefore, the present findings strongly recommended the use of sera to assess the LDH activity and indicate better stability of sera LDH-5 than sera CK during post burn wound healing.

Total lactate dehydrogenase and its isoenzymes in serum in the presence of penicillamine and other sulfhydryl compounds.

1977 ◽  
Vol 23 (2) ◽  
pp. 229-233 ◽  
Author(s):  
L L Gershbein ◽  
K G Raikoff
Keyword(s):  
Lactate Dehydrogenase ◽  
Disc Electrophoresis ◽  
The Other ◽  
Rat Serum ◽  
Initial Concentration ◽  
Ldh Isoenzymes ◽  
Allosteric Effectors ◽  
Sulfhydryl Compounds

Abstract Toward delineation of changes in total lactate dehydrogenase (LDH) and in the distribution of LDH isoenzymes as assessed by polyacrylamide disc electrophoresis, we inbucated human and rat sera with various agents, notably sulfhydryl compounds. Although artefacts were apparent when these agents were used without preliminary adjustment of pH, we saw little alteration in total unitage when one or two volumes of serum was mixed with one volume of any of several thiols, especially penicillamine, at an initial concentration of 0.4 mol/liter and pH 7.0-7.5. Under these conditions, penicillamine caused a loss in LDH-5 after incubation for 1 h at 25 degrees C together with small decreases in mobility of the other four isoenzymes toward the anode. A zymosan region appeared below the albumin and tracking dye area. With longer periods of incubation of rat serum with penicillamine or alpha-mercaptosuccinate, a novel band in the zymogram was noted just above the LDH-4 peak. The observations are discussed in terms of allosteric effectors.

scholarly journals Maternal immune response and air pollution exposure during pregnancy: insights from the Early Markers for Autism (EMA) study

2020 ◽  
Vol 12 (1) ◽  
Author(s):  
Heather E. Volk ◽  
Bo Park ◽  
Calliope Hollingue ◽  
Karen L. Jones ◽  
Paul Ashwood ◽  
...  
Keyword(s):  
Air Pollution ◽  
Intellectual Disability ◽  
Prenatal Screening ◽  
Maternal Serum ◽  
Serum Samples ◽  
Maternal Immune Activation ◽  
Early Markers ◽  
Air Pollution Exposure ◽  
Pollution Exposure ◽  
The Relationship

Abstract Background Perinatal exposure to air pollution and immune system dysregulation are two factors consistently associated with autism spectrum disorders (ASD) and other neurodevelopmental outcomes. However, little is known about how air pollution may influence maternal immune function during pregnancy. Objectives To assess the relationship between mid-gestational circulating levels of maternal cytokines/chemokines and previous month air pollution exposure across neurodevelopmental groups, and to assess whether cytokines/chemokines mediate the relationship between air pollution exposures and risk of ASD and/or intellectual disability (ID) in the Early Markers for Autism (EMA) study. Methods EMA is a population-based, nested case–control study which linked archived maternal serum samples collected during weeks 15–19 of gestation for routine prenatal screening, birth records, and Department of Developmental Services (DDS) records. Children receiving DDS services for ASD without intellectual disability (ASD without ID; n = 199), ASD with ID (ASD with ID; n = 180), ID without ASD (ID; n = 164), and children from the general population (GP; n = 414) with no DDS services were included in this analysis. Serum samples were quantified for 22 cytokines/chemokines using Luminex multiplex analysis technology. Air pollution exposure for the month prior to maternal serum collection was assigned based on the Environmental Protection Agency’s Air Quality System data using the maternal residential address reported during the prenatal screening visit. Results Previous month air pollution exposure and mid-gestational maternal cytokine and chemokine levels were significantly correlated, though weak in magnitude (ranging from − 0.16 to 0.13). Ten pairs of mid-pregnancy immune markers and previous month air pollutants were significantly associated within one of the child neurodevelopmental groups, adjusted for covariates (p < 0.001). Mid-pregnancy air pollution was not associated with any neurodevelopmental outcome. IL-6 remained associated with ASD with ID even after adjusting for air pollution exposure. Conclusion This study suggests that maternal immune activation is associated with risk for neurodevelopmental disorders. Furthermore, that prenatal air pollution exposure is associated with small, but perhaps biologically relevant, effects on maternal immune system function during pregnancy. Additional studies are needed to better evaluate how prenatal exposure to air pollution affects the trajectory of maternal immune activation during pregnancy, if windows of heightened susceptibility can be identified, and how these factors influence neurodevelopment of the offspring.

Extra Lactate Dehydrogenase Isoenzyme Band in Serum of Patients with Severe Liver Disease

1971 ◽  
Vol 17 (9) ◽  
pp. 882-885 ◽  
Author(s):  
T Lubrano ◽  
A A Dietz ◽  
H M Rubinstein
Keyword(s):  
Liver Disease ◽  
Lactate Dehydrogenase ◽  
Serum Bilirubin ◽  
High Serum ◽  
Severe Liver ◽  
Additional Band ◽  
Dehydrogenase Isoenzyme ◽  
Severe Liver Disease ◽  
Isoenzyme Patterns ◽  
High Serum Bilirubin

Abstract In a study of lactate dehydrogenase isoenzyme patterns in the sera of patients with severe liver disease, who were primarily selected because of an abnormally high serum bilirubin, 42 of 76 patients had an additional band (LDH-T) between isoenzymes 4 and 5 on acrylamide gel. Thirty of the 42 patients died during followup, 24 within a month of recognition of the extra band.

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