Purification and characterization of particulate acid phosphatases from eggs of Mediterranean sea urchins

1986 ◽  
Vol 84 (3) ◽  
pp. 255-260 ◽  
Author(s):  
Yukio Yokota
Keyword(s):  
Mediterranean Sea ◽  
Sea Urchins ◽  
Acid Phosphatases ◽  
Purification And Characterization

scholarly journals Phosphatase activity of Poa pratensis seeds. II. Purification and characterization of acid phosphatase Ia2 and Ia3

2015 ◽  
Vol 44 (2) ◽  
pp. 255-263 ◽  
Author(s):  
I. Lorenc-Kubis ◽  
B. Morawiecka ◽  
M. Niezgódka ◽  
A. Hebrowska
Keyword(s):  
Acid Phosphatase ◽  
Mixed Type ◽  
Poa Pratensis ◽  
Maximal Activity ◽  
Molecular Forms ◽  
Acid Phosphatases ◽  
Purification And Characterization ◽  
Inorganic Pyrophosphate ◽  
Nitrophenyl Phosphate

Two acid phosphatases (Ia2, Ia3) have been isolated from <i>Poa pratensis</i> seeds and partially purified. Both enzymes showed maximal activity at pH 4,9. They exhibited high activity towards p-nitrophenyl phosphate, inorganic pyrophosphate and phenyl phosphate, much less activity towards glucose-6 phosphate, and mononucleotides. Phosphatases a<sub>2</sub> and a<sub>3</sub> differed in their activity towards ADP. Orthophosphate, fluoride and Zn<sup>2+</sup> were effective inhibitors. EDTA, β-mercaptoethanol and Mg<sup>2+</sup> activated phophatase a<sub>2</sub> but had no effect on phosphatase a<sub>3</sub>. Zn<sup>2+</sup> inhibited the activity of phosphatase a<sub>2</sub> noncompetitively, whereas phosphatase a<sub>3</sub> showed inhibition of mixed type. Trypsin, chymotrypsin and pronase had no effect on the enzyme activities of both molecular forms.

Purification and characterization of multiple forms of soybean seed acid phosphatases

1998 ◽  
Vol 36 (7) ◽  
pp. 487-494 ◽  
Author(s):  
Carmen Verissima Ferreira ◽  
Jose Mauro Granjeiro ◽  
Eulazio Mikio Taga ◽  
Hiroshi Aoyama
Keyword(s):  
Soybean Seed ◽  
Acid Phosphatases ◽  
Multiple Forms ◽  
Purification And Characterization

Skeletal elements of crinoid echinoderms: High-resolution structural and microanalytical results

1983 ◽  
Vol 41 ◽  
pp. 194-195
Author(s):  
D. F. Blake ◽  
L. F. Allard ◽  
D. R. Peacor
Keyword(s):  
High Resolution ◽  
Marine Invertebrates ◽  
Sea Urchins ◽  
Structural Features ◽  
Sea Stars ◽  
High Resolution Tem ◽  
Relationship Of ◽  
The Relationship ◽  
Insight Into

Echinodermata is a phylum of marine invertebrates which has been extant since Cambrian time (c.a. 500 m.y. before the present). Modern examples of echinoderms include sea urchins, sea stars, and sea lilies (crinoids). The endoskeletons of echinoderms are composed of plates or ossicles (Fig. 1) which are with few exceptions, porous, single crystals of high-magnesian calcite. Despite their single crystal nature, fracture surfaces do not exhibit the near-perfect {10.4} cleavage characteristic of inorganic calcite. This paradoxical mix of biogenic and inorganic features has prompted much recent work on echinoderm skeletal crystallography. Furthermore, fossil echinoderm hard parts comprise a volumetrically significant portion of some marine limestones sequences. The ultrastructural and microchemical characterization of modern skeletal material should lend insight into: 1). The nature of the biogenic processes involved, for example, the relationship of Mg heterogeneity to morphological and structural features in modern echinoderm material, and 2). The nature of the diagenetic changes undergone by their ancient, fossilized counterparts. In this study, high resolution TEM (HRTEM), high voltage TEM (HVTEM), and STEM microanalysis are used to characterize tha ultrastructural and microchemical composition of skeletal elements of the modern crinoid Neocrinus blakei.

Purification and characterization of phosphoglucomutase from peas

1994 ◽  
Vol 92 (3) ◽  
pp. 479-486 ◽  
Author(s):  
Cynthia M. Galloway ◽  
W. Mack Dugger
Keyword(s):  
Purification And Characterization

Purification and Characterization of Tissue-Type Plasminogen Activator in Maxillary Mucosa with Chronic Inflammation

1985 ◽  
Vol 54 (02) ◽  
pp. 485-489 ◽  
Author(s):  
Yukiyoshi Hamaguchi ◽  
Masuichi Ohi ◽  
Yasuo Sakakura ◽  
Yasuro Miyoshi
Keyword(s):  
Plasminogen Activator ◽  
Chronic Inflammation ◽  
Gel Filtration ◽  
Potassium Acetate ◽  
Tissue Type ◽  
Purification And Characterization ◽  
Tissue Type Plasminogen Activator ◽  
Urokinase Inhibitor ◽  
Type Plasminogen Activator

SummaryTissue-type plasminogen activator (TPA) was purified from maxillary mucosa with chronic inflammation and compared with urokinase. Purification procedure consisted of the extraction from delipidated mucosa with 0.3M potassium acetate buffer (pH 4.2), 66% saturation of ammonium sulfate, zinc chelate-Sepharose, concanavalin A-Sepharose and Sephadex G-100 gel filtration chromatographies.The molecular weight of the TPA was approximately 58,000 ± 3,000. Its activity was enhanced in the presence of fibrin and was quenched by placental urokinase inhibitor, but not quenched by anti-urokinase antibody. The TPA made no precipitin line against anti-urokinase antibody, while urokinase did.All these findings indicate that the TPA in maxillary mucosa with chronic inflammation is immunologically dissimilar to urokinase and in its affinity for fibrin.

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