Acid hydrolase activity and cyclic nucleotide content in the rat heart during myocardial ischemia and postischemic reperfusion

1989 ◽  
Vol 108 (1) ◽  
pp. 937-939 ◽  
Author(s):  
T. N. Ivanova ◽  
A. I. Ivanov ◽  
B. F. Korovkin ◽  
N. I. Losev
Keyword(s):  
Myocardial Ischemia ◽  
Cyclic Nucleotide ◽  
Rat Heart ◽  
Hydrolase Activity ◽  
Acid Hydrolase ◽  
Postischemic Reperfusion ◽  
Nucleotide Content

scholarly journals Characterization of triacylglycerol hydrolase activities in isolated myocardial cells from rat heart

1985 ◽  
Vol 232 (1) ◽  
pp. 229-236 ◽  
Author(s):  
I Ramírez ◽  
A J Kryski ◽  
O Ben-Zeev ◽  
M C Schotz ◽  
D L Severson
Keyword(s):  
Ionic Strength ◽  
Subcellular Distribution ◽  
Rat Heart ◽  
High Ionic Strength ◽  
Hydrolase Activity ◽  
Affinity Column ◽  
Acid Hydrolase ◽  
Ph Optimum ◽  
Unbound Fraction ◽  
Triacylglycerol Hydrolase

Triacylglycerol (TG) hydrolase activities were characterized in myocytes isolated from rat hearts. Acid hydrolase activity with a pH optimum of 5 could be measured in myocyte homogenates, and the subcellular distribution suggested that this activity originated in lysosomes. Lipoprotein lipase (LPL) was also present in myocyte homogenates, as evidenced by TG hydrolase activity that was stimulated by serum and apolipoprotein CII, and inhibited by apolipoprotein CIII2, high ionic strength (NaCl and MgCl2, I = 1 M) and antibodies to LPL. Serum-independent neutral (pH 7.5) TG hydrolase activity was less sensitive to inhibition by 1 M-NaCl, by antibodies to LPL and by preincubation at 40 degrees C than was serum-stimulated hydrolase activity. Furthermore, there were modest but significant differences in the subcellular distribution of the serum-independent and serum-stimulated hydrolase activities. Hydrolase activities in myocyte homogenates could be solubilized by 7.2 mM-deoxycholate. Acid hydrolase activity was recovered in the unbound fraction after heparin-Sepharose chromatography, whereas LPL was bound to the affinity column and was eluted by 0.9-1.2 M-NaCl. Approximately one-third of the serum-independent TG hydrolase activity was not bound to the heparin-Sepharose affinity column. This unbound TG hydrolase activity had a pH optimum of 7 and was stimulated by 50 mM-MgCl2, but not by serum and was resistant to inhibition by high ionic strength (1 M-NaCl), to preincubation at 40 degrees C for 2 h, and by antibodies to LPL. It is concluded that, in addition to an acid lysosomal TG hydrolase and LPL, myocytes from rat heart contain a serum-independent TG hydrolase with unique characteristics.

Changes in the cyclic nucleotide content in wound tissues during healing

1979 ◽  
Vol 87 (6) ◽  
pp. 625-627 ◽  
Author(s):  
I. M. Nosova ◽  
M. A. Zaidenberg ◽  
V. N. Petrosova ◽  
R. D. Seifulla ◽  
A. A. Karelin
Keyword(s):  
Cyclic Nucleotide ◽  
Nucleotide Content

Acid Hydrolase Activity in Osteoarthritic and Normal Human Cartilage

1973 ◽  
Vol 55 (5) ◽  
pp. 1068-1076 ◽  
Author(s):  
MICHAEL G. EHRLICH ◽  
HENRY J. MANKIN ◽  
BENJAMIN V. TREADWELL
Keyword(s):  
Hydrolase Activity ◽  
Acid Hydrolase ◽  
Human Cartilage ◽  
Normal Human
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