Analytical applications of the continuous measurement of reaction rate: Lactic dehydrogenase in blood serum

1962 ◽  
Vol 4 (6) ◽  
pp. 476-488 ◽  
Author(s):  
W.J. Blaedel ◽  
G.P. Hicks
Keyword(s):  
Blood Serum ◽  
Reaction Rate ◽  
Continuous Measurement ◽  
Lactic Dehydrogenase ◽  
Analytical Applications

Measurement of Serum Lactic Dehydrogenase

1961 ◽  
Vol 7 (3) ◽  
pp. 265-274 ◽  
Author(s):  
H Alan Ells
Keyword(s):  
Present Method ◽  
Reaction Rate ◽  
Continuous Measurement ◽  
Colorimetric Method ◽  
Lactic Dehydrogenase ◽  
Phenazine Methosulfate ◽  
Ldh Activity ◽  
Serum Lactic Dehydrogenase ◽  
Method Agreement ◽  
Mediate Electron Transfer

Abstract A colorimetric method is described for the measurement of serum lactic dehydrogenase (LDH) activity. The method employs phenazine methosulfate to mediate electron transfer between reduced diphosphopyridine nucleotide and 2,6-dichloroindophenol, and allows continuous measurement of the reaction rate in the direction lactate to pyruvate. The LDH of a number of normal and pathologic sera was measured by the present method and by the ultraviolet spectrophotometric method. Agreement between the two methods is good.

Blood serum enzyme activity of dogs exposed to heat stress and muscular exercise

1965 ◽  
Vol 20 (4) ◽  
pp. 587-590 ◽  
Author(s):  
E. Bedrak
Keyword(s):  
Heat Stress ◽  
Blood Serum ◽  
Lactic Dehydrogenase ◽  
Muscular Exercise ◽  
Control Groups ◽  
Serum Enzyme ◽  
Heat Acclimatization ◽  
Hot Environment ◽  
Ldh Activity ◽  
Before And After

The activity of several clinically important enzymes was determined in 11 Alsatian dogs exercised in a temperate environment, exposed to heat stress alone, and exercised in a hot environment before and after heat acclimatization. Enhanced activities of glutamic oxalacetic transaminase (GOT) (P < 0.01), glutamic pyruvic transaminase (GPT) (P < 0.05), lactic dehydrogenase (LDH), phosphohexose isomerase (PHI) (P < 0.05), acid phosphatase (ACP), alkaline phosphatase (ALP), aldolase (ALD), and lipase (LIP) were observed in all dogs exposed to the various physiological stresses. The alteration in enzyme activities of acclimatized dogs was generally smaller than in nonacclimatized animals. Comparison between the two control groups (heat acclimatized versus nonacclimatized) indicates a significant increase in LDH activity (P < 0.01) and lower activities of PHI (P < 0.05), ACP (P < 0.05), and ALP (P < 0.01) in heat-acclimatized dogs. blood serum enzymes in acute stresses; muscular exercise in a hot environment; nonacclimatized dogs; heat-acclimatized dogs Submitted on August 17, 1964

Specific Enzymatic Determination of Glucose in Blood Serum or Plasma by an Automatic Potentiometric Reaction-Rate Method

1962 ◽  
Vol 8 (6) ◽  
pp. 606-615 ◽  
Author(s):  
H V Malmstadt ◽  
H L Pardue
Keyword(s):  
Blood Serum ◽  
Blood Plasma ◽  
Reaction Rate ◽  
Measurement Time ◽  
Sample Handling ◽  
Enzymatic Determination ◽  
Speed Up ◽  
Rate Method ◽  
Relative Errors

Abstract A new automatic potentiometric reaction-rate method has been applied to the specific enzymatic measurement of glucose in blood plasma or serum. A new filtering technic is described for removal of precipitated protein. The use of injection pipets to simplify and speed up the reagent-and sample-handling step is described. Glucose is determined in 0.02 ml. of serum or plasma with relative errors within 2%. The average measurement time is about 30 sec.

Non-classical hydrogen bond triggered strand displacement for analytical applications and DNA nanostructure assembly

2018 ◽  
Vol 42 (9) ◽  
pp. 6636-6639 ◽  
Author(s):  
Manli Han ◽  
Qingsheng Fan ◽  
Yi Zhang ◽  
Lida Xu ◽  
Changyuan Yu ◽  
...  
Keyword(s):  
Hydrogen Bond ◽  
Reaction Rate ◽  
Cyanuric Acid ◽  
Strand Displacement ◽  
Fast Reaction ◽  
Dna Nanostructure ◽  
Analytical Applications ◽  
Classical Hydrogen Bond ◽  
Fast Reaction Rate

A novel strand displacement triggered by the non-classical hydrogen bond between cyanuric acid and adenine exhibits a fast reaction rate.

Automatic Determination of Lactic Acid in Blood

1969 ◽  
Vol 15 (10) ◽  
pp. 940-948 ◽  
Author(s):  
T P Hadjiioannou ◽  
P A Siskos ◽  
C G Valkana
Keyword(s):  
Lactic Acid ◽  
Reaction Rate ◽  
Lactic Dehydrogenase ◽  
Lactic Acid Concentration ◽  
Automatic Determination ◽  
Fixed Amount ◽  
Rate Method ◽  
Relative Errors ◽  
Time Required

Abstract An automatic reaction rate method is described for the determination of lactic acid in blood. The L(+)-lactic acid is selectively oxidized in the presence of lactic dehydrogenase and diphosphopyridine nucleotide to form an absorbing species. The time required for the formation of a fixed amount of DANH is measured automatically and related directly to the lactic acid concentration. The method is sensitive, more rapid than purely chemical procedures, and relative errors are only about 1-3% for the range 6-200 µg of lactic acid. The coefficient of variation for the determination of lactic acid in 0.2 ml of blood is 3%. Measurement times vary from a few seconds to about 2 min.

Interface Instrumentation between Computer and Spectrophotometer for Reaction Rate Measurements

1970 ◽  
Vol 16 (3) ◽  
pp. 215-221 ◽  
Author(s):  
E Clifford Toren ◽  
Arthur A Eggert ◽  
Arletta E Sherry ◽  
G Phillip Hicks
Keyword(s):  
Reaction Rate ◽  
Clinical Laboratory ◽  
Lactic Dehydrogenase ◽  
Input Voltage ◽  
Rate Of Change ◽  
Test Results ◽  
Laboratory Computer ◽  
Voltage Level ◽  
Accuracy And Precision ◽  
Software Changes

Abstract An instrument interface which generates an output voltage level proportional to rate of change of an input voltage is described. The interface permits direct connection of routine spectrophotometric rate measurements to a real-time laboratory computer system. The form of the voltage level output enables the computer to read rates in the same manner as peaks are read for AutoAnalyzers, permitting the clinical laboratory LABCOM system to compute and report results for rate methods with no software changes. Spectrophotometric rates from about 10 to 0.025 absorbance units per min can be measured with an accuracy and precision of less than 1% relative in measurement times of about 10 to 30 s, respectively. The interface is readily constructed from commercially available components. Test results are presented for simulated rates, lactic dehydrogenase, and alkaline phosphatase.

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