[25] Routine analysis with immobilized enzyme nylon tube reactors

1988 ◽  
pp. 288-297 ◽  
Author(s):  
P.V. Sundaram
Keyword(s):  
Immobilized Enzyme ◽  
Routine Analysis ◽  
Nylon Tube

Routine glucose determination in serum by use of an immobilized glucose dehydrogenase nylon-tube reactor.

1979 ◽  
Vol 25 (8) ◽  
pp. 1436-1439 ◽  
Author(s):  
P V Sundaram ◽  
B Blumenberg ◽  
W Hinsch
Keyword(s):  
Solution Method ◽  
Immobilized Enzyme ◽  
Glucose Dehydrogenase ◽  
Serum Glucose ◽  
Glucose Determination ◽  
Tube Reactor ◽  
Nylon Tube ◽  
The Cost ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Continuous Use

Abstract We report a method for immobilizing glucose dehydrogenase on the inside surface of nylon tubes to produce an immobilized-enzyme nylon-tube reactor. The glucose dehydrogenase reactor is integrated into the flow system of a continuous-flow analyzer to facilitate routine analysis of serum glucose at 50 samples/h. We compared results with those by the reference hexokinase/glucose-6-phosphate dehydrogenase solution method. The coefficient of correlation was r = 0.996. A glucose dehydrogenase reactor made starting with 1 mg (250 U) of enzyme was stable during eight weeks of continuous use, that is, for nearly 3500 tests. This reduced the cost of the assay by at least 50-fold, compared with that for a commercial glucose dehydrogenase test pack method.

Immobilized-enzyme nylon-tube reactor for routine determination of uric acid in serum.

1978 ◽  
Vol 24 (10) ◽  
pp. 1813-1817 ◽  
Author(s):  
P V Sundaram ◽  
M P Igloi ◽  
R Wassermann ◽  
W Hinsch
Keyword(s):  
Clinical Trials ◽  
Uric Acid ◽  
High Precision ◽  
Lower Cost ◽  
Immobilized Enzyme ◽  
Tube Reactor ◽  
Nylon Tube ◽  
Flow Through

Abstract We report here the preparation of an immobilized-enzyme nylon-tube reactor containing uricase (EC 1.7.3.3) and the assembly of a flow-through system (Technicon AutoAnalyzer II) for the routine determination of uric acid in serum. Results of these uric acid analyses by use of immobilized uricase, in conjunction with peroxidase (EC 1.11.1.7) and aminophenazone-dichlorophenol in solution, are compared with those obtained with the same enzyme in solution by use of the uricase-PAP (peroxidase, 4-aminophenazone, dichlorophenol) method. Clinical trials carried out routinely with the uricase reactor give reliable and reproducible results with high precision at an appreciably lower cost. The reactors are stable to continued or intermittent use for at least three months or for 4000 tests.

scholarly journals Immobilized-enzyme pipette. Scope and limitations of a simple device

1979 ◽  
Vol 179 (2) ◽  
pp. 445-447 ◽  
Author(s):  
P V Sundaram
Keyword(s):  
Immobilized Enzyme ◽  
Inside Surface ◽  
Simple Device ◽  
New Development ◽  
Nylon Tube

Disposable pipette tips made of polymeric nylon tube with enzymes bound covalently to their inside surface and fixed to the stem of an automatic, adjustable-volume pipette holder together constitutes an immobilized enzyme pipette or ‘Impette’. The present paper describes the application in research laboratories and clinics of this new development, with urease as an example in the determination of blood urea.

Immobilized-enzyme nylon-tube reactors for routine determination of urea and citrulline in serum.

1978 ◽  
Vol 24 (2) ◽  
pp. 234-239 ◽  
Author(s):  
P V Sundaram ◽  
M P Igloi ◽  
R Wassermann ◽  
W Hinsch ◽  
K J Knoke
Keyword(s):  
Solution Method ◽  
Immobilized Enzyme ◽  
Low Cost ◽  
System A ◽  
Tube Reactor ◽  
Nylon Tube ◽  
Diacetyl Monoxime ◽  
Flow Through ◽  
Continued Use

Abstract A continuous-flow clinical analyzer for the routine estimation of urea is described that makes use of an immobilized-enzyme nylon-tube reactor as part of a flow-through system (a Technicon AutoAnalyzer I). Results of blood-urea analyses by use of the immobilized urease are compared with determinations made with the diacetyl monoxime method and the urease solution method. Clinical trials carried out routinely with the immobilized enzyme nylon tube reactor give reliable and reproducible results with high precision and low cost. The reactors are stable to intermittent or continued use for at least four months or for 2000 tests. A method is described in which differential colorimetry is used for determining citrulline in blood and which makes use of the immobilized urease, albeit indirectly.

Interactive multiple area spectrum integration (MASI)

1994 ◽  
Vol 52 ◽  
pp. 942-943
Author(s):  
John A. Hunt ◽  
Richard D. Leapman ◽  
David B. Williams
Keyword(s):  
Image Processing ◽  
Low Dose ◽  
Routine Analysis ◽  
Reference Image ◽  
Area Spectrum ◽  
List Type ◽  
Type Number ◽  
Image Processor ◽  
X Ray ◽  
Scanning Path

Interactive MASI involves controlling the raster of a STEM or SEM probe to areas predefined byan integration mask which is formed by image processing, drawing or selecting regions manually. EELS, x-ray, or other spectra are then acquired while the probe is scanning over the areas defined by the integration mask. The technique has several advantages: (1) Low-dose spectra can be acquired by averaging the dose over a great many similar features. (2) MASI can eliminate the risks of spatial under- or over-sampling of multiple, complicated, and irregularly shaped objects. (3) MASI is an extremely rapid and convenient way to record spectra for routine analysis. The technique is performed as follows:Acquire reference imageOptionally blank beam for beam-sensitive specimensUse image processor to select integration mask from reference imageCalculate scanning path for probeUnblank probe (if blanked)Correct for specimen drift since reference image acquisition

On the Preparation of Bovine α-Thrombin

1978 ◽  
Vol 39 (01) ◽  
pp. 193-200 ◽  
Author(s):  
Erwin F Workman ◽  
Roger L Lundblad
Keyword(s):  
Immobilized Enzyme ◽  
Catalytic Properties ◽  
Specific Activity ◽  
Guanidine Hydrochloride ◽  
Low Molecular Weight ◽  
Reversible Process ◽  
Gel Beads ◽  
Tissue Thromboplastin ◽  
C 50 ◽  
Hydrolysis Of

SummaryAn improved method for the preparation of bovine α-thrombin is described. The procedure involves the activation of partially purified prothrombin with tissue thromboplastin followed by chromatography on Sulfopropyl-Sephadex C-50. The purified enzyme is homogeneous on polyacrylamide discontinuous gel electrophoresis and has a specific activity toward fibrinogen of 2,200–2,700 N.I.H. U/mg. Its stability on storage in liquid media is dependent on both ionic strenght and temperature. Increasing ionic strength and decreasing temperature result in optimal stability. The denaturation of α-thrombin by guanidine hydrochloride was found to be a partially reversible process with the renatured species possessing properties similar to “aged” thrombin. In addition, the catalytic properties of a-thrombin covalently attached to agarose gel beads were also examined. The activity of the immobilized enzyme toward fibrinogen was affected to a much greater extent than was the hydrolysis of low molecular weight, synthetic substrates.

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