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Biomedical subjects

U Rosa

Publications and source records attributed to U Rosa.

At least 37 records · Page 2Linked to original sources
PubMed1969

Iodination of insulin in aqueous and organic solvents.

1. The iodination of insulin was studied under various experimental conditions in aqueous media and in some organic solvents, by measuring separately the uptake of iodine by the four tyrosyl groups and the relative amounts of monoiodotyrosine and di-iodotyrosine that are formed. In aqueous media from pH1 to pH9 the iodination occurs predominantly on the tyrosyl groups of the A chain. Some organic solvents increase the iodine uptake of the B-chain tyrosyl groups. Their efficacy in promoting iodination of Tyr-B-16 and Tyr-B-26 is in the order: ethylene glycol and propylene glycol approximately methanol and ethanol>dioxan>8m-urea. 2. It is suggested that each of the four tyrosyl groups in insulin has a different environment: Tyr-A-14 is fully exposed to the solvent; Tyr-A-19 is sterically influenced by the environmental structure, possibly by the vicinity of a disulphide interchain bond; Tyr-B-16 is embedded into a non-polar area whose stability is virtually independent of the molecular conformation; Tyr-B-26 is probably in a situation similar to Tyr-B-16 with the difference that its non-polar environment depends on the preservation of the native structure.

Chemical Phenomena↗
PubMed1968

The effect of chemical modifications induced in insulin on the reactivity of the interchain disulphide bonds towards sodium sulphite.

The reactivity of the three disulphide bridges of insulin towards sodium sulphite was studied by amperometric titration of the liberated thiol groups. In the native, acetylated or succinylated molecule two bridges react at pH7, but in the methylated or phenylcarbamoylated molecule only one bridge reacts. All three bridges react in all derivatives in 8m-urea or at pH9. Loss in biological activity parallels the loss in reactivity of one of the bridges during methylation. It is suggested that change in reactivity of the S.S bonds reflects the occurrence of a conformational modification of the protein. The possibility is discussed that the unusually high reactivity of the S.S bonds in native insulin depends strictly on the integrity of the native molecule, suggesting that S.S bonds are in some way involved in the hormone's mode of action.

Acetates↗
PubMed1967

Effect of the insulin iodination on the reactivity of the inter-chain disulphide bonds towards sodium sulphite.

Insulin iodination interferes with the ability of the interchain S.S bonds to react with sulphite at pH7. In insulin samples containing more than 5 iodine atoms/monomer unit, only one S.S bond/molecule reacts. The effect must be related to the substitution of the iodine into the tyrosyl groups, which probably causes a conformational rearrangement resulting in a steric hindrance of one of the interchain S.S bonds. The effect is removed by increasing the pH or by adding urea (8m) to the reaction mixture. The unreactivity of the S.S bond and the biological inactivation occur at the same ;critical' iodination level, suggesting that a same primary alteration of the molecule is responsible for both the effects.

Animals↗
PubMedDate not supplied

CT findings in hemitruncus.

Origin of the right pulmonary artery from the ascending aorta is a rare congenital malformation resulting in a large left-to-right shunt through the right lung at systemic pressure. We report the CT findings in an adult with this anomaly. Computed tomography was diagnostic. The patient is the sixth adult with this condition reported in the literature.

Adult↗