A rapid method for separation and detection of human salivary amylase isoenzymes by isoelectric focusing in polyacrylamide gel

1976 ◽  
Vol 84 (4) ◽  
pp. 234-239
Author(s):  
TORKEL WADSTRÖM ◽  
CARL-ERIK NORD ◽  
MARIANNE KJELLGREN
Keyword(s):  
Rapid Method ◽  
Isoelectric Focusing ◽  
Polyacrylamide Gel ◽  
Salivary Amylase ◽  
Amylase Isoenzymes

A rapid method for isoelectric focusing in polyacrylamide gel

FEBS Letters ◽  
1972 ◽  
Vol 24 (1) ◽  
pp. 89-92 ◽  
Author(s):  
J. Söderholm ◽  
P. Allestam ◽  
T. Wadström
Keyword(s):  
Rapid Method ◽  
Isoelectric Focusing ◽  
Polyacrylamide Gel

Isoelectric focusing of insulin, 125I-insulin and the 125I-insulin-antibody complex

1979 ◽  
Vol 44 (6) ◽  
pp. 1828-1834
Author(s):  
Asja Šiševa ◽  
Jiřina Slaninová ◽  
Tomislav Barth ◽  
Stephan P. Ditzov ◽  
Luben M. Sirakov
Keyword(s):  
Isoelectric Focusing ◽  
Polyacrylamide Gel ◽  
The Other ◽  
Insulin Antibody ◽  
Isoelectric Points ◽  
Antibody Complex ◽  
And Storage ◽  
Acid Region ◽  
Three Components

Isoelectric focusing on polyacrylamide gel columns of three native crystalline commercial preparations of insulin and 125I-labelled insulin was carried out. All the compounds studied contained three components of different isoelectric points. The largest fraction, having pI 5.60 ± 0.05, was common to all preparations. The other two fractions were situated in the acid region of pH between pI 4.5 and 5.2. The presence of these fractions is explained by the contamination of crystalline insulins by proinsulin and by the formation of des-amido derivatives during the dissolving and storage of insulin samples, and, in case of labelled insulin, also by the presence of heavily iodinated insulin and contaminating components. The isoelectric focusing of the complex 125I-insulin-antibody showed a peak of radioactivity having pI 6.15 ± 0.05.

scholarly journals Mechanism of methaemoglobin reduction by human erythrocytes

1980 ◽  
Vol 188 (2) ◽  
pp. 535-540 ◽  
Author(s):  
A Tomoda ◽  
M Ida ◽  
A Tsuji ◽  
Y Yoneyama
Keyword(s):  
Methylene Blue ◽  
Isoelectric Focusing ◽  
Rate Constants ◽  
Time Course ◽  
Reaction Rate ◽  
Polyacrylamide Gel ◽  
Human Erythrocytes ◽  
Redox Potentials ◽  
Reaction Rate Constants ◽  
Beta 2

The time course of methaemoglobin reduction in human erythrocytes treated with nitrite was studied at pH 7.4, 37 degrees C, in the presence or absence of Methylene Blue, and the changes in methaemoglobin, intermediate haemoglobins and oxyhaemoglobin during the reaction were analysed by isoelectric-focusing on Ampholine/polyacrylamide-gel plates. In both cases, with or without the dye, the intermediate haemoglobins were found to be present at (alpha 3+beta 2+)2 and (alpha 2+beta 3+)2 valency hybrids from their characteristic position on electrophoresis, but amounts changed consecutively with time. The amount of (alpha 3+beta 2+)2 was always greater than that of the (alpha 2+beta 3+)2 valency hybrid. This result is explained by the differences in redox potentials between alpha- and beta-chains in methaemoglobin tetramer. It was concluded that methaemoglobin was reduced in human erythrocytes through these two different pats: methaemoglobin leads to k+3 (alpha 2+beta 3+)2 leads to k+3 oxyhaemoglobin. The reaction rate constants k'+1 (= k+1+k+3) and k'+2(=k+2+k+4) were estimated from the changes in each component methaemoglobin, intermediate haemoglobins [(alpha 3+beta 2+)2+(alpha 2+beta 3+)2] and oxyhaemoglobin.

scholarly journals ANALYSIS OF SHEEP HEMOGLOBINS BY ISOELECTRIC FOCUSING IN POLYACRYLAMIDE-GEL

1983 ◽  
Vol 1983 (11) ◽  
pp. 39-42
Author(s):  
Masaharu KOTANI ◽  
Kenji TSUNODA ◽  
Tatsuro SHIMAOKA
Keyword(s):  
Isoelectric Focusing ◽  
Polyacrylamide Gel

Quantitative gel-electrophoretic determination of serum amylase isoenzyme distributions.

1979 ◽  
Vol 25 (11) ◽  
pp. 1919-1923 ◽  
Author(s):  
B K Gillard
Keyword(s):  
Differential Diagnosis ◽  
Disease Progression ◽  
Quantitative Method ◽  
Serum Amylase ◽  
Soluble Starch ◽  
Normal Serum ◽  
Polyacrylamide Gel ◽  
Starch Solution ◽  
Amylase Isoenzymes

Abstract I report a direct, sensitive, quantitative method for determining serum amylase isoenzyme activity with commercially available reagents. Day-to-day reproducibility (CV) was 3--4% for the isoenzymes in normal serum; within-run precision was 8, 3, and 2% for low, normal and high isoenzyme activities. Amylase isoenzymes, separated into the pancreatic and salivary types by electrophoresis in polyacrylamide gel, are then quantified by directly incubating the gels in soluble-starch solution, staining with iodine, and densitometry. The proportion of pancreatic isoenzyme (47 normal sera) was 43 +/- 8% (mean +/- SD). Isoenzyme activities as low as 2% of normal can be measured accurately in 10 micro L of serum. The reproducibility, precision, and sensitivity indicate that the method is applicable to differential diagnosis of hyperamylasemia or hypoamylasemia, and is suited for monitoring the subtle changes in serum amylase isoenzyme distribution that may accompany disease progression or therapy.

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