Acid phosphatases in the frog (Rana esculenta) skeletal muscle. Purification and some properties of the low molecular weight enzyme

Panara, Fausto; Angiolillo, Antonella; Secca, Teresa; Rosa, Ines Di; Fagotti, Anna; Pascolini, Rita

doi:10.1016/0020-711x(91)90152-d

Cited by 8 publications

(2 citation statements)

References 32 publications

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“…On the other hand, glycerol and methanol enhanced the phosphatase activity two±three times. Similar activation has been observed with several low molecular weight TyrPase/acid phosphatase preparations (Taga and Van Etten, 1982;Panara et al, 1991), and was explained in terms of phosphotransferase activity. Tartrate and NaF, which are potent inhibitors of high molecular weight acid phosphatases, showed little effect, while EDTA and okadaic acid, classical inhibitors of phosphoserine/threonine protein phosphatases, were also ineffective.…”

Section: Effects Of Various Inhibitors and Activators On Phosphatase supporting

confidence: 67%

18 kDa Protein Tyrosine Phosphatase in the Ocular Lens

Umeda

Kashiwa

Nishigori

2001

Experimental Eye Research

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Section: Effects Of Various Inhibitors and Activators On Phosphatase supporting

confidence: 67%

18 kDa Protein Tyrosine Phosphatase in the Ocular Lens

Umeda

Kashiwa

Nishigori

2001

Experimental Eye Research

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“…Two mammalian isoenzymes share the conserved Nand C-terminal sequences, separated by a variable region of34 residues (17)(18)(19)(20)(21)(22). Phosphatases showing similar molecular masses and some common enzymatic properties are reportedly present in lower vertebrates, although no sequence information is available for them (23)(24)(25). Initially identified as acid phosphatases, the low M; PTPases have since been shown to exhibit catalytic activity in vitro toward phosphotyrosyl, but not phosphoseryl or phosphothreonyl, proteins and peptides (11,14,26,27).…”

Section: The Nucleotide Sequencers) Reported In This Paper Has Been Submittedmentioning

confidence: 99%

Cloning and Characterization of a Saccharomyces cerevisiae Gene Encoding the Low Molecular Weight Protein-tyrosine Phosphatase

Ostanin

Pokalsky

Wang

et al. 1995

Journal of Biological Chemistry

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The low molecular weight protein-tyrosine phosphatase (low M(r) PTPase) is an 18-kDa cytoplasmic enzyme of unknown function that has been previously found in several vertebrates. Using an oligonucleotide probe derived from the active site sequence of the mammalian low M(r) PTPases, a Saccharomyces cerevisiae gene that encodes a homolog of this enzyme was cloned by low stringency hybridization. This gene, LTP1, together with a neighboring gene, TKL1, is shown to be located on the right arm of chromosome XVI. The deduced amino acid sequence of its 161-amino acid residue product shows a 39% average identity with that of the mammalian enzymes. The yeast Ltp1 protein was expressed in Escherichia coli, purified to homogeneity, and shown to possess PTPase activity. The recombinant Ltp1 efficiently hydrolyzes phosphotyrosine and a phosphotyrosine-containing peptide, Tyr531-fyn, but it shows low activity toward phosphoserine and phosphothreonine. The catalytic activity of Ltp1 toward a number of substrates was approximately 30-fold lower than the corresponding values measured for the bovine low M(r) PTPase. However, the yeast enzyme was markedly activated by adenine and some purine nucleosides and nucleotides, including cAMP and cGMP. In the case of adenine, the activity of Ltp1 was increased by approximately 30-fold. The high degree of evolutionary conservation of the low M(r) PTPases implies a significant role for this enzyme. However, neither the disruption of the LTP1 gene nor an approximately 10-fold overexpression of its product in S. cerevisiae caused any apparent phenotypic changes under the conditions tested. No proteins related to Ltp1 could be detected in extracts of the ltp1 null mutant, either by immunoblotting or by gel-filtration analysis accompanied by extended kinetic assays, consistent with the conclusion that LTP1 is the only low M(r) PTPase-encoding gene in S. cerevisiae.

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The Molecular Basis of The “Red Cell” Acid Phosphatase Polymorphism

Dissing

1994

Advances in Forensic Haemogenetics

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Acid phosphatases in the frog (Rana esculenta) skeletal muscle. Purification and some properties of the low molecular weight enzyme

Cited by 8 publications

References 32 publications

18 kDa Protein Tyrosine Phosphatase in the Ocular Lens

18 kDa Protein Tyrosine Phosphatase in the Ocular Lens

Cloning and Characterization of a Saccharomyces cerevisiae Gene Encoding the Low Molecular Weight Protein-tyrosine Phosphatase

The Molecular Basis of The “Red Cell” Acid Phosphatase Polymorphism

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