A microlagal-based carbonaceous sensor for enzymatic determination of glucose in blood serum

2021 ◽  
Author(s):  
Seyed Mostafa Jafari ◽  
Saeed Masoum ◽  
Seyed Ali Hosseini Tafreshi
Keyword(s):  
Blood Serum ◽  
Enzymatic Determination

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.

Enzymatic Determination of Hydroxysteroids in Human Skin Surface Lipids1

1963 ◽  
Vol 41 (5) ◽  
pp. 265-268 ◽  
Author(s):  
Thomas J Cook ◽  
Allan L Lorincz ◽  
Alan R Spector
Keyword(s):  
Human Skin ◽  
Skin Surface ◽  
Enzymatic Determination

Polarographic study of hydrolysis of [8-lysine]vasopressin and its derivatives with blood serum of pregnant women

1980 ◽  
Vol 45 (4) ◽  
pp. 1099-1108 ◽  
Author(s):  
Mikuláš Chavko ◽  
Michal Bartík ◽  
Evžen Kasafírek
Keyword(s):  
Blood Serum ◽  
Pregnant Women ◽  
Degree Of Hydrolysis ◽  
Polarographic Study ◽  
Ph Optimum ◽  
Lysine Vasopressin ◽  
Rate Of Hydrolysis ◽  
Hydrolysis Of ◽  
Vasopressin Analogues

A polarographic study of the hydrolysis of [8-lysine]vasopressin and some hormonogens of the vasopressin series with the blood serum of women in the last week of pregnancy was studied. The dependence of hydrolysis on pH (pH optimum: 7.4-7.50, substrate concentration (Km 1.2 . 10-5M), pH stability and thermal stability were determined. The rate of hydrolysis of individual vasopressin analogues decreases in the order: [8-lysine]vasopressin > Nα-glycyl-prolyl[8-lysine]-vasopressin > Nα-leucyl-[8-lysine]vasopressin > Nα-alanyl-[8-lysine]vasopressin > Nα-phenyl alanyl-[8-lysine]vasopressin > Nα-diglycyl-[8-lysine]vasopressin > Nα-prolyl-[8-lysine]vasopressin > Nα-triglycyl-[8-lysine]vasopressin > Nα-sarcosyl-glycyl-[8-lysine]vasopressin. The degree of hydrolysis gradually increases to a multiple with the length of the pregnancy in consequence of the presence of oxytocine. However, vasopressin is also hydrolysed to a small extent with the enzymes from the blood sera of non-pregnant women. Under similar analytical conditions oxytocin was not hydrolysed with the sera of non-pregnant women and therefore oxytocin is a more suitable substrate than vasopressin for polarographic determination of serum oxytocinase.

Enzymatic colorimetry of lecithin and sphingomyelin in aqueous solution.

1983 ◽  
Vol 29 (8) ◽  
pp. 1513-1517 ◽  
Author(s):  
M W McGowan ◽  
J D Artiss ◽  
B Zak
Keyword(s):  
Aqueous Solution ◽  
Hydrogen Peroxide ◽  
Amniotic Fluid ◽  
Enzymatic Reaction ◽  
Detergent Solution ◽  
Enzymatic Determination ◽  
Red Color ◽  
Hydrolysis Of ◽  
Zwitterionic Detergent

Abstract A procedure for the enzymatic determination of lecithin and sphingomyelin in aqueous solution is described. The phospholipids are first dissolved in chloroform:methanol (2:1 by vol), the solvent is evaporated, and the residue is redissolved in an aqueous zwitterionic detergent solution. The enzymatic reaction sequences of both assays involve hydrolysis of the phospholipids to produce choline, which is then oxidized to betaine, thus generating hydrogen peroxide. The hydrogen peroxide is subsequently utilized in the enzymatic coupling of 4-aminoantipyrine and sodium 2-hydroxy-3,5-dichlorobenzenesulfonate, an intensely red color being formed. The presence of a non-reacting phospholipid enhances the hydrolysis of the reacting phospholipid. Thus we added lecithin to the sphingomyelin standards and sphingomyelin to the lecithin standards. This precise procedure may be applicable to determination of lecithin and sphingomyelin in amniotic fluid.

Non-enzymatic determination of purine nucleotides using a carbon dot modified glassy carbon electrode

2019 ◽  
Vol 11 (30) ◽  
pp. 3866-3873 ◽  
Author(s):  
R. Karthikeyan ◽  
D. James Nelson ◽  
S. Abraham John
Keyword(s):  
Glassy Carbon ◽  
Low Cost ◽  
Phosphate Buffer Solution ◽  
Purine Nucleotides ◽  
Buffer Solution ◽  
Solution Ph ◽  
Carbon Dot ◽  
Enzymatic Determination ◽  
Sensitive Determination

Selective and sensitive determination of one of the purine nucleotides, inosine (INO) using a low cost carbon dot (CD) modified glassy carbon (GC) electrode in 0.2 M phosphate buffer solution (pH 7.2) was demonstrated in this paper.

Sign in / Sign up

Export Citation Format

Share Document