On the isoenzymes of human red cell acid phosphatase

Kaczmarek, M

doi:10.1016/0006-2944(76)90021-1

Cited by 6 publications

(2 citation statements)

References 10 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…of 14 800 (Fisher & Harris, 1971) indicates that the enzymes are not identical. Although the acid phosphatase tends to form dimers and tetramers (Kaczmarek, 1976), it can be excluded, on account of their different molecular weights, that the enzymes are identical.…”

Section: Discussionmentioning

confidence: 99%

Partial purification and characterization of human erythrocyte phosphoglycollate phosphatase

Zecher¹,

Wolf²

1980

Biochemical Journal

View full text Add to dashboard Cite

Human erythrocytes contain a phosphatase that is highly specific for phosphoglycollate. It shows optimum pH of 6.7 and has Km 1 mM for phosphoglycollate. The molecular weight appears to be about 72000. The enzyme is a dimeric molecule having subunits of mol. wt. about 35000. It could be purified approx. 4000-fold up to a specific activity of 5.98 units/mg of protein. The activity of the enzyme is Mg2+-dependent. Co2+, and to a smaller extent Mn2+, may substitute for Mg2+. Half-maximum inhibition of the phosphatase by 5,5'-dithiobis-(2-nitrobenzoate), EDTA and NaF is obtained at 0.5 microM, 1 mM and 4 mM respectively. Moreover, it needs a univalent cation for optimum activity. Phosphoglycollate phosphatase is a cytoplasmic enzyme. Approx. 5% of its total activity is membrane-associated. This part of activity can be approx. 70% solubilized by freezing, thawing and treatment with 0.25% Triton X-100.

show abstract

Section: Discussionmentioning

confidence: 99%

Partial purification and characterization of human erythrocyte phosphoglycollate phosphatase

Zecher¹,

Wolf²

1980

Biochemical Journal

View full text Add to dashboard Cite

show abstract

“…This important relationship between the isoenzyme pattern and enzyme activity of serum prostate acid phosphatase warrants further investigation. Since acid phosphatase is biochemically of glycoprotein nature [8,9], these isoenzymes of serum prostate acid phosphatase may represent sialoproteins containing various amounts of neuraminic acid residues. After incubation of serum with neuraminidase, the original eight isoenzymes were shown (fi- Figure 2.…”

Section: Resultsmentioning

confidence: 99%

Isoenzymes of Human Prostate Acid Phosphatase

Chu¹,

Wang²,

Merrin³

et al. 1978

Oncology

View full text Add to dashboard Cite

The isoenzymes of human prostatic acid phosphatase have been studied by an isoelectric focusing technique. Purified acid phosphatase from malignant prostates contained eight isoenzymes with pI 4.4–5.3. The sera from patients with prostate cancer were shown to have similar acid phosphatase isoenzyme patterns at pI 4.0–5.5; as the serum enzyme activities increased, the pI of isoenzymes shifted to more acidic pH. These isoenzyme patterns of sera from patients with prostate cancer were different from those of patients with Gaucher’s disease or from acid phosphatase of human erythrocytes, both of which exhibited only one enzyme band around pI 5.0 and 6.0, respectively. Treatment of serum sample of prostate cancer with neuraminidase did not result in a single enzyme band but alter the pI of isoenzymes, which shifted to a higher pH region. The significance of acid phosphatase activities and its isoenzyme patterns in prostate cancer merits further investigation.

show abstract

Human erythrocyte cytosol phosphatidyl-inositol-bisphosphate phosphatase

Roach

Palmer

1981

Biochimica et Biophysica Acta (BBA) - Enzymology

View full text Add to dashboard Cite

On the isoenzymes of human red cell acid phosphatase

Cited by 6 publications

References 10 publications

Partial purification and characterization of human erythrocyte phosphoglycollate phosphatase

Partial purification and characterization of human erythrocyte phosphoglycollate phosphatase

Isoenzymes of Human Prostate Acid Phosphatase

Human erythrocyte cytosol phosphatidyl-inositol-bisphosphate phosphatase

Contact Info

Product

Resources

About