Acid phosphatases

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Acid phosphatases and seed shriveling in triticale.

Seed shriveling in the man-made intergeneric hybrid, triticale (x Triticosecale Wittmack) appears to be related to increased activity of endosperm acid phosphatases including para-nitrophenyl phosphatase, ATPase, ADPase, phosphatidic phosphatase, and glucose-1-phosphatase that occur specifically at later stages of seed development. These hydrolases may reduce endogenous substrates for starch sy...

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Revisiting histidine-dependent acid phosphatases: a distinct group of tyrosine phosphatases.

Although classical protein tyrosine phosphatase (PTP) superfamily members are cysteine-dependent, emerging evidence shows that many acid phosphatases (AcPs) function as histidine-dependent PTPs in vivo. These AcPs dephosphorylate phospho-tyrosine substrates intracellularly and could have roles in development and disease. In contrast to cysteine-dependent PTPs, they utilize histidine, rather tha...

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Differential Expression of Arabidopsis thaliana Acid Phosphatases in Response to Abiotic Stresses

The objective of this research is to identify Arabidopsis thaliana genes encoding acid phosphatases induced by phosphate starvation. Multiple alignments of eukaryotic acid phosphatase amino acid sequences led to the classification of these proteins into four groups including purple acid phosphatases (PAPs). Specific primers were degenerated and designed based on conserved sequences of PAPs isol...

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Purification and Characterization of Two Acid Phosphatases from Germinating Peanut (Arachis hypogaea) Seed

The maximum acid phosphatasic activity was detected in peanut seed at the 5th day of germination. At least, two acid phosphatases were purified by successive chromatography separations on DEAE-Sepharose CL-6B, CM-Sepharose CL-6B, Sephacryl S-100 HR, and Phenyl-Sepharose HP to apparent homogeneity from five days old cotyledon of peanut after germination. These isoenzymes, designated peanut cotyl...

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ژورنال

عنوان ژورنال: Molecular Pathology

سال: 2002

ISSN: 1366-8714

DOI: 10.1136/mp.55.2.65