POTENTIOMETRIC BEHAVIOR OF AQUEOUS SOLUTIONS OF MALEIC ACID-STYRENE COPOLYMER WITH ADDED BIVALENT METAL IONS

1978 ◽  
Vol 7 (10) ◽  
pp. 1173-1176 ◽  
Author(s):  
Fumitaka Yamashita ◽  
Tsuyoshi Komatsu ◽  
Tsurutaro Nakagawa
Keyword(s):  
Aqueous Solutions ◽  
Metal Ions ◽  
Maleic Acid ◽  
Bivalent Metal ◽  
Styrene Copolymer ◽  
Bivalent Metal Ions

Adsorptions of Some Heavy Metal Ions in Aqueous Solutions by Acrylamide/Maleic Acid Hydrogels

1995 ◽  
Vol 30 (17) ◽  
pp. 3287-3298 ◽  
Author(s):  
Dursun Saraydin ◽  
Erdener Karadağ ◽  
Olgun Güven
Keyword(s):  
Heavy Metal ◽  
Aqueous Solutions ◽  
Metal Ions ◽  
Maleic Acid ◽  
Heavy Metal Ions

scholarly journals Separation and properties of two arylamidases from rat cardiac-muscle extracts

1977 ◽  
Vol 163 (3) ◽  
pp. 565-570 ◽  
Author(s):  
A F Bury ◽  
T Coolbear ◽  
C R Savery
Keyword(s):  
Metal Ions ◽  
Cardiac Muscle ◽  
Rat Heart ◽  
Bivalent Metal ◽  
Ph Optimum ◽  
Minor Peak ◽  
Bivalent Metal Ions ◽  
Stimulation Of

Two main arylamidase activities were separated from a particle-free supernatant of rat heart by chromatography on DEAE-Sephadex. Although both enzymes hydrolysed L-leucine 4-nitroanilide, only peak-II enzyme hydrolysed L-lysine 4-nitroanilide. A third minor peak (Ia) contained an enzyme that was active mainly on the L-lysine 4-nitroanilide. The mol.wts. of the enzymes in peaks I and II were approx. 257000 and 105000 respectively. The pH optimum was approx. pH7.0 for peak-I enzyme and 7.0-8.0 for peak-II enzyme. Both enzymes were inhibited by addition of puromycin, p-hydroxymercuribenzoate, o-phenanthroline and bivalent metal ions. Addition of dithiothreitol resulted in stimulation of both activities. Dialysis against o-phenanthroline resulted in inhibition of peak-I and -II enzymes, but after dialysis against EDTA only peak-II enzyme was inhibited.

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