Labelling of human fibrinogen with 131I by electrolytic iodination

Rosa, U.; Scassellati, G. A.; Pennisi, F.; Riccioni, N; Giagnoni, P; Giordani, Roberto

doi:10.1016/0304-4165(64)90091-1

Cited by 168 publications

(35 citation statements)

References 14 publications

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“…The inter-and intra-assay coefficients of variation were 14 and 7%, respectively (18), in the range of the basal concentrations (3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18)(19)(20) ,uU/ml). …”

Section: Methodsmentioning

confidence: 99%

Kinetic Analysis of Plasma Insulin Disappearance in Nonketotic Diabetic Patients and in Normal Subjects

Navalesi¹,

Pilo²,

Ferrannini³

et al. 1978

J. Clin. Invest.

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A B S T R A C Tson with normals (172 +14); these differences reflected the different basal plasma insulin concentrations in these three groups. Chronic treatment with oral hypoglycemic drugs, age, duration of the disease, and degree of metabolic control appeared to have only little effect on the kinetics of insulin. On the basis of these results, we conclude that insulin-independent adult diabetics show, already in the fasting state, a combination of insulin resistance and insulin deficiency and a derangement in insulin distribution, the precise significance of which is uncertain.

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Section: Methodsmentioning

confidence: 99%

Kinetic Analysis of Plasma Insulin Disappearance in Nonketotic Diabetic Patients and in Normal Subjects

Navalesi¹,

Pilo²,

Ferrannini³

et al. 1978

J. Clin. Invest.

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“…IgG was separated from the IgG-rich fractions by chromatography on DEAE-cellulose using 0.02 m phosphate buffer, pH 8, for equilibration and elution [15]; the albumen was further purified by chromatography using 0.02 m acetate buffer for equilibrium and elution [17], followed by gel filtration on Sephadex G-100. The IgG and albumen were then radioactively labelled with 131I, and 125I, respective ly [16] and the radioactivities of all experimental samples determined by means of a Panax double-channel scintillation counter.…”

Section: Radioactively Labelled Proteinsmentioning

confidence: 99%

Studies <i>in vivo</i> and <i>in vitro</i> of the Transfer of Rat IgG and Rat Albumen Across the Intestinal Walls of Young Rats

Jones¹

1974

Neonatology

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Preparations of radioactively labelled rat albumen and IgG have been fed together in equal concentrations to 3-, 14- and 24-day-old rats. Quantitative experiments showed that both proteins were absorbed at 3 days of age, but by the 14th day, the transmission of rat albumen had ceased. No proteins were absorbed by 24-day-old rats. Gel filtration studies of the intra-lumenal contents collected 30 min after feeding have demonstrated clear differences in the relative gastric digestion of the administered proteins. In marked contrast to the in vivo studies, it has been shown that everted intestinal sacs prepared from 14- and 24-day-old rats are able to transport both rat albumen and IgG in vitro, significantly more of the former than of the latter protein being transferred under the given experimental conditions.

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“…The fibrinogen was labelled with Iz5I, using the iodine monocl. !oride method (12) or the electrolytic iodination method of Rosa et al (17). The labelled preparations had a coagulability of 90-93 % of the protein and the iodination was calculated to be <0.5 atoms per molecule fibrinogen.…”

Section: Materials a N D Methodsmentioning

confidence: 99%

Inhibitory Effect of Dextran 40 upon Thrombin-induced Fibrin Deposition in Rat Lungs

Diffang¹,

Rammer²,

Saldeen³

1976

Upsala Journal of Medical Sciences

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The effect of dextran 40 upon thrombin-induced fibrin deposition in rat lungs was studied. A quantitative method employing isotope-labelled fibrinogen was used to determine the amount of fibrin in the lungs. It was shown that pretreatment with dextran 40 suppressed the accumulation of fibrin in the lungs after iqjection of thrombin. This was not due to redistribution of the fibrin to other organs but appeared to be a result of decreased intravascular coagulation. It seemed unlikely that the finding could be explained by an effect of dextran upon fibrinolysis.

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Labelling of human fibrinogen with 131I by electrolytic iodination

Cited by 168 publications

References 14 publications

Kinetic Analysis of Plasma Insulin Disappearance in Nonketotic Diabetic Patients and in Normal Subjects

Kinetic Analysis of Plasma Insulin Disappearance in Nonketotic Diabetic Patients and in Normal Subjects

Studies <i>in vivo</i> and <i>in vitro</i> of the Transfer of Rat IgG and Rat Albumen Across the Intestinal Walls of Young Rats

Inhibitory Effect of Dextran 40 upon Thrombin-induced Fibrin Deposition in Rat Lungs

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