scholarly journals FLUORIMETRIC DETERMINATION OF CREATINE KINASE ACTIVITY IN ISOLATED SINGLE NEURONS

1973 ◽  
Vol 21 (6) ◽  
pp. 568-571 ◽  
Author(s):  
IGOR B. KRASNOV
Keyword(s):  
Creatine Kinase ◽  
Enzyme Activity ◽  
Coefficient Of Variation ◽  
Kinase Activity ◽  
Tissue Sample ◽  
Vestibular Nucleus ◽  
Creatine Kinase Activity ◽  
Single Neurons ◽  
Fluorimetric Determination

A quantitative fluorimetric method for determination of creatine kinase activity in isolated single nerve cells (2-10 ng dry weight) has been developed. Enzyme activity was measured in the direction of adenosine triphosphate and creatine formation. The creatine generated was measured by the fluorescent compound formed with ninhydrin in alkali. The coefficient of variation for the assay of enzyme activity in brain homogenate (47 ng wet tissue/sample) was 3.17%. The coefficient of variation for single neurons of the lateral vestibular nucleus (nucleus Deitersi) in rabbit was about 15%. The creatine kinase activity in these cell bodies was 342.0 ± 14.2 moles/kg dry tissue/hr, at 38°C.

Effects of Ca, Mg, and EDTA on creatine kinase activity in cerebrospinal fluid.

1979 ◽  
Vol 25 (1) ◽  
pp. 147-150 ◽  
Author(s):  
P Urdal ◽  
J H Strømme
Keyword(s):  
Cerebrospinal Fluid ◽  
Creatine Kinase ◽  
Enzyme Activity ◽  
Kinase Activity ◽  
Creatine Kinase Activity ◽  
Precise Estimate ◽  
The Relationship ◽  
Sample Fraction ◽  
Sensitive Method

Abstract For one to obtain a precise estimate of creatine kinase (CK) activity in cerebrospinal fluid, the sample fraction is increased by about 10-fold over that used for serum. This increases the concentration of interfering substances, Ca being especially important. Therefore, the relationship between Ca, Mg, and EDTA was examined. Enzyme activity was maximal with 15 mmol of Mg per liter in the presence of 3 mmol of EDTA per liter, otherwise according to the (Scandinavian) recommended conditions for determination of CK activity in serum. These modifications increased the activity of CK by 35% for CK-MM and by 60% for CK-BB. Counteraction of Ca-induced inhibition was the main reason to this increase. We describe a practical and sensitive method for determining CK in cerebrospinal fluid.

Bioluminescence flow sensor for determination of creatine kinase activity in blood

1989 ◽  
Vol 227 ◽  
pp. 29-36 ◽  
Author(s):  
S. Girotti ◽  
M.L. Cascione ◽  
S. Ghini ◽  
G. Carrea ◽  
R. Bovara ◽  
...  
Keyword(s):  
Creatine Kinase ◽  
Kinase Activity ◽  
Creatine Kinase Activity ◽  
Flow Sensor

Causes of Increased Plasma Creatine Kinase Activity after Surgery

1974 ◽  
Vol 20 (3) ◽  
pp. 340-342 ◽  
Author(s):  
Kannika S Phornphutkul ◽  
Sinn Anuras ◽  
Raymond S Koff ◽  
Leonard B Seeff ◽  
Donald L Mahler ◽  
...  
Keyword(s):  
Creatine Kinase ◽  
Enzyme Activity ◽  
Drug Exposure ◽  
Kinase Activity ◽  
Clinical Evidence ◽  
Creatine Kinase Activity ◽  
Drug Reactions ◽  
Ornithine Carbamoyl Transferase ◽  
Elective Surgical Procedures ◽  
Plasma Creatine Kinase

Abstract To determine whether drug reactions might play a role in postoperatively increased plasma enzyme activity, we measured creatine kinase (CK), and ornithine carbamoyl transferase (OCT) activities immediately before and on the 1st, 4th, and 8th day after 343 elective surgical procedures performed on 327 patients who had received various drugs pre-operatively. We saw no overt clinical evidence of muscle damage, but plasma CK activity was significantly increased on the first postoperative day. Plasma OCT activity was not significantly altered. We found no relationship between prior drug exposure and in creased CK activity, but the administration of general rather than regional anesthesia and the duration of anesthesia during surgery were closely related to increased CK activity. Halothane or succinylcholine administration during operation was also associated with a significant increase in CK activity in subjects whose pre-operative CK activity was normal. In contrast, subjects with increased pre-operative CK activities did not show this response to halothane or succinylcholine.

Evaluation of a New Procedure for Measuring Serum Creatine Kinase Activity

1970 ◽  
Vol 16 (5) ◽  
pp. 370-374 ◽  
Author(s):  
J Henry Wilkinson ◽  
B Steciw
Keyword(s):  
Creatine Kinase ◽  
Spectrophotometric Method ◽  
Kinase Activity ◽  
Creatine Phosphate ◽  
Sample Volume ◽  
Creatine Kinase Activity ◽  
Serum Creatine Kinase ◽  
Normal Range ◽  
Glucose 6 Phosphate Dehydrogenase

Abstract A new spectrophotometric microtechnique for the determination of serum creatine kinase activity, in which all reagents are provided in a single com-pressed tablet, has been evaluated. The procedure depends upon coupling the creatine phosphate-ADP reaction with the hexokinase and glucose-6-phosphate dehydrogenase reactions. The new technique is quick, relatively simple, and gives results which compare favorably with the conventional spectrophotometric method in precision and sensitivity. It requires a sample volume of 10 Al, and values ranging from 10 to1600 U/liter can be determined without dilution. Gross hemolysis leads to erroneously high values, but the error is negligible with slightly hemolyzed specimens. A provisional normal range has been established

Observations on the Fluorometric Measurement of Creatine Kinase Activity

1968 ◽  
Vol 14 (7) ◽  
pp. 660-663 ◽  
Author(s):  
Sylvan M Sax ◽  
John J Moore
Keyword(s):  
Creatine Kinase ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Kinase Activity ◽  
Creatine Kinase Activity ◽  
High Background ◽  
Phosphatase Activities ◽  
Background Fluorescence ◽  
Significant Difference

Abstract Twenty patients’ serums have been analyzed by both the Sax-Moore (1) and Conn-Anido (2) creatine kinase methods. No significant difference in enzyme activity was found. In our hands, the Conn-Anido procedure, as originally described, gave variable results and high background fluorescence. The presence of high alkaline or acid phosphatase activities in specimens analyzed by the Sax-Moore procedure does not cause spurious elevations of creatine kinase.

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