Abnormal Electrophoretic Patterns of Extractable Proteins and Enzymes (Isozymes) in Human Brain Tumors.

Gerhardt, W.; Clausen, J.; Christensen, Ernst; Riishede, J; Munch‐Petersen, Jon

doi:10.3891/acta.chem.scand.17-0875

Cited by 3 publications

(3 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Bands 5 and 8 are similar in electrophsretic n-aobility and behavior to bands sf A-esterase activity observed by Barrsn et at. (8), but differ slightly in ~a~obility from the A-esterase of hun~ara seruaar (14).…”

Section: Discussionmentioning

confidence: 99%

“…The electrophoretic mobility of the brain acid plaosphatase is similar to bands observed in liver (lo), skeletal ~ssuscEe (12), and heart (13). Gerhardt et al detected two zones of acid phosphatase by agar gel electrophoresis, but did nnot test %he possibility sf substrate hydrolysis h y other ernzymes (8). Alkaline phosphatase is absent in t h e eIectrsphsretically separated extracts of brain thsuglt its presence in brain has been dennolastrated E~istolsgically (33, 34).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Properties and Classification of the Soluble Esterases of Human Brain

Ecobichon¹

1966

Can. J. Physiol. Pharmacol.

View full text Add to dashboard Cite

I%iater-soluble proteins and enzymes of human brain were separated by vertical zone electrophoresis in starch gel. Fifteen bands of esterase activity were detected in brain. Various substrates and inhibitors were used in efforts to identify enzymes in addition to a comparison caf the esteras pattern with patterns obtained from other human tissues. 0116 zone, conaposed of four bands of acetylesterase activity, was found to be conlmon t o all the tissues investigated with the exceptioi~ of serum. ' H' wo bands of choliriesterase and two bards of A-esterase activity were identified. The remaitring bands, which were aliesterases possessirig broad overlapping substrate specificity and inhibitor sensitivity, were eiectrophsretically differerat from thsse of other tissues. Observatio~~s on alkaline phosphatase, acid phosphataue, and lactate dehydrogenase were recorded for conaparison with the data an esterases.The colxaplexity of the esterase activity of Inlaman brain has been investigated with techniques s f differential inhibition and substrate specificity (1-5). The esterases which have been identified include aeetylcholinesterase (1,4), butyryleholinesterase (2,4), a Ca++-dependent arylesterase (A-esterase) ( 3 ) , arad nonspecific esterases which hydrolyze phenyl acetate and phenyl butyrate (3).Several publicatio~~s have described the electrophoretic separation of specific and nonspecific brain esterases in various supporting media (6-8). A paper recently published by Barrsn et ak. (9) was nf particular interest because the brain esterases showed electrophoretic patterns sirni%ar to those observed in this labsratesrg-; for esterases separated from extracts of other human tissues (10-13). The present investigations evere carried out t s compare the electrophoretically separated esterases of human brain with thsse observed by sther workers and to correlate these enzgrnles with those found in other tissues sf the human Isody. MethodsSamples from different-regions of the human brain were obtained at autopsy and were frozen immediately upon removal. The tissue was either used a t once s r stored a t -20 "C until just before use. Hamogenatea of white and gray ~natter (separate or mixed) were prepared in distilled water in a 1:2 dilution (grams wet tissue per milliliter water) with a DuaEI homogenizer maintained at approximately 4 "C in a bath sf ice water. The hamogenates were frozen and thawed several times and were then centrifuged in a refrigerated centrifuge a t 35,000 g for 7 ' 5 minutes. The supernatants \%yere removed by pipette, placed

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Properties and Classification of the Soluble Esterases of Human Brain

Ecobichon¹

1966

Can. J. Physiol. Pharmacol.

View full text Add to dashboard Cite

show abstract

“…In a certain tissue population the LDH pattern may change as a function of developmental factors (Clausen & Hustrulid, 1969), but it can also be altered by malignant transformation (Gerhardt, Clausen, Christensen & Riishede, 1967) and by change in functional state of the tissue (Philip & Vesell, 1962). To elucidate some of the factors altering the LDH isoenzyme pattern, kidney-cortex tubule cells were cultivated under different environmental conditions.…”

mentioning

confidence: 99%

Factors affecting the lactate dehydrogenase isoenzyme pattern of cultured kidney-cortex cells

Güttler¹,

Clausen²

1969

Biochemical Journal

View full text Add to dashboard Cite

1. The lactate dehydrogenase isoenzyme pattern of cultured calf kidney-cortex cells was correlated to growth phase, changes in oxygen supply, mean generation time and changes in nutritional supply. 2. During culture of free cells and intact explants the lactate dehydrogenase isoenzyme pattern changed towards a dominance of isoenzymes containing the M subunit. 3. Of the shift in monomer proportion, 58% occurred during the lag phase and 42% during the initial part of the exponential growth phase. During the stationary phase the shift in monomer proportion reversed slightly. It was possible to relate the observed shift in monomer proportion to the glycolytic rate. 4. Factors that depressed glycolysis decreased the shift in monomer proportion. Oxygen was found to limit the decrease in the Hsubunit/Msubunit ratio caused by anaerobic culture in vitro. 5. The results obtained support the view that the altered lactate dehydrogenase isoenzyme pattern of urine in renal ischaemia may be explained by anaerobic changes in the lactate dehydrogenase isoenzyme pattern of cortical tubule cells.

show abstract

Isoenzymes in Cancer

Turner

1964

Proceedings of the Association of Clinical Biochemists

View full text Add to dashboard Cite

With the development of techniques for the qualitative and quantitative study of isoenzymes (Latner and Skillen, 1961; Van der Helm, Zondag and Klein, 1963; Gerhardt, 1963 et al;Richterich, Schafroth and Aebi, 1963) some attention has been drawn to a study of isoenzymes in cancer. We have been studying isoenzymes of lactate dehydrogenase, leucine aminopeptidase, and alkaline phosphatase chiefly, using starch-gel electrophoresis. The gel buffer used is Tris-HCl 0·025 M, pH 8·6 and by this method five zones of activity of LDH and three zones for LAP can be well separated.A study of isoenzymes in cancer sera has, as have enzyme determinations, shown no ' cancer specific changes' though distributions are sometimes abnormal. For example, LAP shows three zones of activity, in contrast to the normal one, in cases of lymphosarcoma (Kowlessar, Haeffner and Riley, 1961), obstructive jaundice secondary to tumour, metastatic carcinoma to the liver and sometimes in cancer of the gastrointestinal tract.Other body fluids show abnormalities of distribution in cancer, for example, in malignant effusions LD 1 and LD 2 (the slowest migrating isoenzymes of LDH in our nomenclature) account for more than 30 % of the total LDH (Richterich, Locher, Zuppinger and Rossi, 1962). Characteristic distributions have also been reported in CSF LDH in some cases of metastatic carcinoma to the brain (van der Helm, Zondag and Klein, 1963).The isoenzymes of tumour tissues show a marked uniformity of pattern when similar amounts of activity are used. With regard to LDH, tumour tissues show predominantly LDl> LD 2 and LD a • When compared with normal adult tissues the tumour tissues show a shift to the slower migrating zones (those associated with aerobic glycolysis). Foetal tissue extracts are very similar to tumour tissues in isoenzyme distribution.Abnormal isoenzymes are sometimes detected in tumours though they are not common, and similar abnormalities can be detected in foetal tissues. Abnormal LDH isoenzymes are usually present in the LD a region and preliminary studies on crude isoenzyme preparations (Starkweather and Schoch, 1962) have shown a difference in Michaelis constants for tumour LD a and normal adult LD a which suggests that the former may be a structurally different protein.

show abstract

Abnormal Electrophoretic Patterns of Extractable Proteins and Enzymes (Isozymes) in Human Brain Tumors.

Cited by 3 publications

References 0 publications

Properties and Classification of the Soluble Esterases of Human Brain

Properties and Classification of the Soluble Esterases of Human Brain

Factors affecting the lactate dehydrogenase isoenzyme pattern of cultured kidney-cortex cells

Isoenzymes in Cancer

Contact Info

Product

Resources

About