Molecular weight differences in acid phosphatases of stem homogenates from L and S flax genotrophs

1983 ◽  
Vol 21 (3-4) ◽  
pp. 391-404 ◽  
Author(s):  
Mary Ann Fieldes ◽  
Hugh Tyson
Keyword(s):  
Molecular Weight ◽  
Acid Phosphatases ◽  
Flax Genotrophs

DIFFERENCES IN MOLECULAR WEIGHT BETWEEN CORRESPONDING ANIONIC PEROXIDASE ISOZYMES FROM TWO FLAX GENOTROPHS

1980 ◽  
Vol 22 (4) ◽  
pp. 529-534 ◽  
Author(s):  
H. Tyson ◽  
M. A. Fieldes
Keyword(s):  
Molecular Weight ◽  
Linear Regression ◽  
Linum Usitatissimum ◽  
Gel Electrophoresis ◽  
Relative Mobility ◽  
Anionic Peroxidase ◽  
Linum Usitatissimum L ◽  
Peroxidase Isozymes ◽  
Flax Genotrophs ◽  
Adult Plants

Anionic peroxidase isozymes from main stem tissues of adult plants of two flax (Linum usitatissimum L.) genotrophs were separated using acrylamide gel electrophoresis. A range of seven acrylamide concentrations was used for the gels, enabling the effect of gel concentration on relative mobility (Rm) to be examined. The regression of log (Rm) on gel concentration was linear for two of the four main isozymes found. Differences in linear regression slope between the L and S flax genotroph isozymes suggested genotroph differences in molecular weight.

Molecular weight and net charge of peroxidase isozymes in F1 hybrids between L and S flax genotrophs

1982 ◽  
Vol 20 (9-10) ◽  
pp. 919-927 ◽  
Author(s):  
Hugh Tyson ◽  
Mary Ann Fieldes
Keyword(s):  
Molecular Weight ◽  
F1 Hybrids ◽  
Net Charge ◽  
Peroxidase Isozymes ◽  
Flax Genotrophs

scholarly journals Two distinct low-molecular-weight acid phosphatases from rat liver.

1988 ◽  
Vol 36 (8) ◽  
pp. 3020-3026 ◽  
Author(s):  
SADAKI FUJIMOTO ◽  
KAZUKI MURAKAMI ◽  
AKIRA ISHIKAWA ◽  
KENJI HIMI ◽  
AKIRA OHARA
Keyword(s):  
Molecular Weight ◽  
Rat Liver ◽  
Low Molecular Weight ◽  
Acid Phosphatases

Characterization of Multiple Acid Phosphatases in Salt-Stressed Spinach Leaves

1987 ◽  
Vol 14 (2) ◽  
pp. 117 ◽  
Author(s):  
SM Pan
Keyword(s):  
Molecular Weight ◽  
Salt Stress ◽  
Gel Electrophoresis ◽  
Spinacia Oleracea ◽  
Acid Phosphatases ◽  
Multiple Forms ◽  
Spinacia Oleracea L ◽  
Hydroponically Grown ◽  
Spinach Leaves

Incremental salt stress brought about a clear enhancement of the activity of acid phosphatases in hydroponically grown spinach (Spinacia oleracea L.) leaves. Sephacryl S-200 chromatography of the enzyme fraction revealed multiple forms of acid phosphatases of high (300 000), intermediate (100 000), and low (35 000) molecular weight in control and salt-stressed spinach leaves. A similar zymogram of acid phosphatases, showing at least six bands in polyacrylamide disc gel electrophoresis, was observed for control and stressed leaves. However, promotive effects of incremental salt stress on the activity of acid phosphatases were more pronounced in high molecular weight acid phosphatases. Substrate specificity and differential effects of some ions on the multiple acid phosphatases were also examined for control and salt-stressed leaves.

Acid Phosphatases Associated With Phosphorus Deficiency in Wheat: Partial Purification and Properties

1991 ◽  
Vol 18 (6) ◽  
pp. 615 ◽  
Author(s):  
RE Guthrie ◽  
KD Mclachlan ◽  
DGD Marco
Keyword(s):  
Molecular Weight ◽  
Phosphorus Deficiency ◽  
Size Exclusion ◽  
Partial Purification ◽  
Acid Phosphatases ◽  
Ammonium Sulfate Precipitation ◽  
Con A ◽  
Substrate Utilisation ◽  
Purification And Properties ◽  
Exclusion Chromatography

Procedures for the partial purification of two phosphatase isozymes found in phosphorus deficient wheat plants are given. The method employs ammonium sulfate precipitation and hydroxylapatite, Con A-Sepharose, anion exchange and size exclusion chromatography. Measurements of their Km, Vmax, pI and molecular weight are reported. Evidence is provided that there are empirical differences in substrate utilisation between these phosphatase isozymes associated with phosphorus deficient plants.

Human liver acid phosphatases: Cysteine residues of the low-molecular-weight enzyme

1982 ◽  
Vol 216 (2) ◽  
pp. 512-521 ◽  
Author(s):  
Piotr M. Laidler ◽  
Eulazio M. Taga ◽  
Robert L. Van Etten
Keyword(s):  
Molecular Weight ◽  
Human Liver ◽  
Cysteine Residues ◽  
Low Molecular Weight ◽  
Acid Phosphatases

scholarly journals Characterization of High- and Low-Molecular Weight Zinc-Dependent Acid Phosphatases in Bovine Liver.

1998 ◽  
Vol 21 (11) ◽  
pp. 1218-1221 ◽  
Author(s):  
Junji TSUDA ◽  
Takanobu KIMURA ◽  
Hiroko TANINO ◽  
Shun SHIMOHAMA ◽  
Sadaki FUJIMOTO
Keyword(s):  
Molecular Weight ◽  
Bovine Liver ◽  
Low Molecular Weight ◽  
Acid Phosphatases

The high molecular weight and the low molecular weight acid phosphatases of the frog liver and their phosphotyrosine activity

1988 ◽  
Vol 90 (1) ◽  
pp. 173-178 ◽  
Author(s):  
Hanna Jańska ◽  
Aleksandra Kubicz ◽  
Agata Szalewicz ◽  
Joanna Haraźna
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Low Molecular Weight ◽  
Acid Phosphatases

scholarly journals Effect of phosphate levels on the synthesis of acid phosphatases (EC 3.1.3.2) inNeurospora crassa

1985 ◽  
Vol 45 (3) ◽  
pp. 239-249 ◽  
Author(s):  
Sergio A. Rodrigues ◽  
Antonio Rossi
Keyword(s):  
Molecular Weight ◽  
Type Strain ◽  
Wild Type Strain ◽  
Deae Cellulose ◽  
Phosphate Starvation ◽  
Acid Phosphatases ◽  
Wild Type ◽  
Specific Activities ◽  
Phosphate Medium ◽  
High Phosphate

SummaryWhen grown on high-phosphate medium, the wild-type strain 74A ofN. crassasynthesized two acid phosphatases, as shown by DEAE -cellulose chromatography. These purified enzymes showed heterogeneity on PAGE, low specific activities towards PNP-P, molecular weight values of at least 300000, no deviation from Michaelian behaviour, and great stability in 50 mM sodium acetate buffer, at pH 5·4, when kept at 54 °C. These acid phosphatases were synthesized in reduced amounts or not at all when the mould was grown under conditions of phosphate starvation, indicating that the level of phosphate also regulates the synthesis of the high molecular weight enzyme forms. When grown on high phosphate medium, thepho-3mutant strain also synthesized two acid phosphatases, whose purified enzymes showed no pronounced differences when compared to those synthesized by the wild-type strain in terms of electrophoretic analysis, specific activities towards PNP-P, molecular weight values, and Michaelian behaviour. However, one enzyme form had a higherKmvalue and a lower heat stability than the corresponding enzyme of the wild-type strain. Even though thepho-3locus might not be responsible for an alteration in the primary structure of the repressible acid phosphatase, it seems clear that the enzymes synthesized by the mould grown on low-or high-phosphate medium must share some structural features. Thus, the drastic differences observed in the molecular properties of the enzymes synthesized by the mould grown under conditions of phosphate starvation as opposed to phosphate repression might be due to an effect exerted by the level of inorganic phosphate in regulating the translation, post-translational modifications and/or excretion, but not necessarily the gene-directed synthesis of distinct mRNAs.

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