Combination of insulin chains on an anti-insulin antibody–Sepharose column

Nature ◽  
1976 ◽  
Vol 262 (5571) ◽  
pp. 791-793 ◽  
Author(s):  
MECHTHILD KLOTZ ◽  
BERND GUTTE
Keyword(s):  
Insulin Antibody ◽  
Sepharose Column ◽  
Insulin Chains

scholarly journals Precipitin reactions between insulin, proinsulin, insulin chains and insulin antibody

Diabetologia ◽  
1973 ◽  
Vol 9 (5) ◽  
pp. 384-386 ◽  
Author(s):  
D. D. Bansal ◽  
J. H. Connolly ◽  
J. Vallance-Owen
Keyword(s):  
Insulin Antibody ◽  
Insulin Chains

Sites of Insulin Action Using Ferritin Labeling

1971 ◽  
Vol 29 ◽  
pp. 540-541
Author(s):  
Burton B. Silver ◽  
Ronald S. Nelson
Keyword(s):  
Electron Microscopy ◽  
Binding Sites ◽  
Anterior Pituitary ◽  
Insulin Action ◽  
Diabetic Rats ◽  
Insulin Antibody ◽  
Fat Pad ◽  
Target Organs ◽  
Uranium Salts ◽  
Sugar Levels

Some investigators feel that insulin does not enter cells but exerts its influence in some manner on the cell surface. Ferritin labeling of insulin and insulin antibody was used to determine if binding sites of insulin to specific target organs could be seen with electron microscopy.Alloxanized rats were considered diabetic if blood sugar levels were in excess of 300 mg %. Test reagents included ferritin, ferritin labeled insulin, and ferritin labeled insulin antibody. Target organs examined were were diaphragm, kidney, gastrocnemius, fat pad, liver and anterior pituitary. Reagents were administered through the left common carotid. Survival time was at least one hour in test animals. Tissue incubation studies were also done in normal as well as diabetic rats. Specimens were fixed in gluteraldehyde and osmium followed by staining with lead and uranium salts. Some tissues were not stained.

PLACENTAL TRANSFER OF INSULIN-131I IN GUINEA PIGS IMMUNIZED AGAINST INSULIN

1966 ◽  
Vol 52 (2) ◽  
pp. 276-291 ◽  
Author(s):  
Jan I. Thorell
Keyword(s):  
Plasma Concentration ◽  
Guinea Pigs ◽  
Placental Transfer ◽  
Maternal Plasma ◽  
Insulin Antibodies ◽  
Insulin Antibody

ABSTRACT The placenta is considered to be impermeable or only slightly permeable to insulin. Insulin antibodies are transferred from mother to foetus in man and in guinea pigs. The passage of insulin-131I from mother to foetus was studied in guinea pigs with and without antibodies against insulin. Antibody-bound insulin-131I was recovered in plasma from foetuses of immunized pregnant guinea pigs, at intervals of more than 5 hours after the injection of insulin-131I to the mother. The foetal levels of insulin-131I were rather low, the highest recorded value being 27% of the maternal plasma concentration. This peak was reached 32 hours after the injection. No insulin-131I was found in the foetuses of non-immunized guinea pigs.

Relation between insulin antibody and complement-fixing islet cell antibody at clinical diagnosis of IDDM

Diabetes ◽  
1986 ◽  
Vol 35 (5) ◽  
pp. 620-622 ◽  
Author(s):  
J. Karjalainen ◽  
M. Knip ◽  
A. Mustonen ◽  
J. Ilonen ◽  
H. K. Akerblom
Keyword(s):  
Clinical Diagnosis ◽  
Islet Cell ◽  
Islet Cell Antibody ◽  
Insulin Antibody ◽  
Cell Antibody

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.

Activation of latent collagenase from polymorphonuclear leukocytes by cathepsin G

1979 ◽  
Vol 44 (10) ◽  
pp. 3177-3182 ◽  
Author(s):  
Mária Stančíková ◽  
Karel Trnavský
Keyword(s):  
Affinity Chromatography ◽  
Trypsin Inhibitor ◽  
Polymorphonuclear Leukocytes ◽  
Soya Bean ◽  
Cathepsin G ◽  
Sepharose Column ◽  
Bean Trypsin Inhibitor ◽  
Human Polymorphonuclear Leukocytes

Cathepsin G was isolated from human polymorphonuclear leukocytes and purified by affinity chromatography on Antilysin-Sepharose column. Purified enzyme activated later collagenase isolated from leukocytes. Activation at 36°C was maximal after 30 min incubation. Inhibitors of cathepsin G - soya-bean trypsin inhibitor, diisopropyl phosphofluoridate and Antilysin were active in inhibiting the activation of latent collagenase by cathepsin G.

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