Ferment-Aktivit�ts-Bestimmungen in der menschlichen Leber

Schmidt, E.; Schmidt, Florian; Wildhirt, E

doi:10.1007/bf01486383

Cited by 49 publications

(16 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…For the proteins of the soluble fractions, a much more considerable error must be expected than for the structure-bound proteins. With the extraction by Potter-Elvejhem after centrifugation for 20 min at 12,500 g, Schmidt et al [15] retrieved 84 ±24 mg protein from the supernatant of the normal liver specimen taken by needle biopsy, and 61.2 ±15.4 mg/g wet wt. from that of acute hepatitis subjects.…”

Section: Discussionmentioning

confidence: 99%

Alkaline Phosphatase in the Subcellular Fractions of Normal and Damaged Human Liver

Massarrat¹

1971

Enzyme

View full text Add to dashboard Cite

During the procedure of the differential centrifugation of small specimens of liver taken by blind needle biopsy, a loss of extractable protein appeared. The loss occurred only in the soluble 12,500 g fraction of the liver and amounted to 38% thereof, compared to a specimen 7 times as heavy, taken at laparotomy. The activity of alkaline phosphatase was increased in all subcellular fractions of the liver in acute hepatitis, chronic hepatitis, and obstructive jaundice, but not in fatty liver, as compared with the control. The main part of the enzyme is localized in the nonsoluble fractions of the liver (nucleus-free 600 g and mitochondrial fractions). The correlation between the activity of alkaline phosphatase in the sera and that in the subcellular fractions of the inflamed noncholestatic liver was poor. The affinity of enzyme from different fractions for the substrate p-nitrophenylphosphate is identical.

show abstract

Section: Discussionmentioning

confidence: 99%

Alkaline Phosphatase in the Subcellular Fractions of Normal and Damaged Human Liver

Massarrat¹

1971

Enzyme

View full text Add to dashboard Cite

show abstract

“…The determination of the intracellular distribution of enzymes and of its alter ations under pathologic conditions is, however, feasible with liver tissue obtained by biopsy due to the techniques of fractionated extraction, differential centrifugation or to methods of iso-enzyme separation [168,169,192,199,207]. But with autopsy material it is hardly possible to obtain quantitative cell fractions of satisfactory purity, because of agonal and post-mortem alterations of permeability [102,214].…”

Section: Intracellular Distribution Of Enzymesmentioning

confidence: 99%

“…As a consequence to injury, on the other hand, the protein content also decreases in absolute terms due in part to a loss into the extracellular medium and to the reduction of protein syn thesis (table IX). [98,197,207] mg/g wet wt …”

Section: Extractable Proteinmentioning

confidence: 99%

Enzyme Activities in Human Liver

Schmidt

1970

Enzymol Biol Clin

Self Cite

View full text Add to dashboard Cite

show abstract

“…Serum-enzymes: amylase [27], caeruloplasmin [28], cholinesterase [29], S-G-O-Transaminase [14], S-G-P-Transaminase [40], and alkaline phosphatase [30], Red cell enzymes: lactic-dehydrogenase [18], glucose-6-phosphate-dehydrogenase [39], hexokinase [31] and fructose-1-6-phosphate-aldolase [24]. All spectrophotometric NAD determi nations have been performed with an Eppendorf Photometer at 366 mp in combination with a recorder.…”

Section: (2) Analysis Of Enzyme Activity In Serum Lysed Red Cells Anmentioning

confidence: 99%

Observations in two Swiss Families with Acatalasia

Aebi¹,

Jeunet²,

Richterich³

et al. 1962

Enzymol Biol Clin

View full text Add to dashboard Cite

(1) In two Swiss families 8 acatalatic and 30 hypocatalatic subjects have been found. Whereas blood catalase activity varies in hypocatalatic subjects from 16-85% of normal, a small but distinct residual activity has been found in acatalatics. This corresponds to 0.1-1.3% of normal activity and does not differ from blood catalase of normal subjects in respect to electrophoretic mobility and azide sensitivity. (2) All acatalatic subjects are in a good state of health. The analysis of their blood in respect to serum, red cell and white cell enzyme patterns revealed no or only minor differences, except that catalase is lacking in the white cells, too. In contrast to normal red cells, those from acatalatic subjects are unable to perform peroxidatic oxidation reactions in the presence of a suitable H202 donor. (3) Intact red cells from acatalatic humans - like those from the duck - exert an exceptionally high rate of methemoglobin formation when exposed to X-rays; it is 10-20 times higher than that in normal human red cells. Addition of small amounts of catalase before irradiation reduces the rate to that of normal.

show abstract

Ferment-Aktivit�ts-Bestimmungen in der menschlichen Leber

Cited by 49 publications

References 23 publications

Alkaline Phosphatase in the Subcellular Fractions of Normal and Damaged Human Liver

Alkaline Phosphatase in the Subcellular Fractions of Normal and Damaged Human Liver

Enzyme Activities in Human Liver

Observations in two Swiss Families with Acatalasia

Contact Info

Product

Resources

About