Search results for "Human insulin"
showing 4 items of 4 documents
Positron Annihilation in Medical Substances of Insulin
2005
Positrons lifetimes were measured in medical substances of insulin (human and animal), differing as far as the degree of purity and time of their activity in the organism are concerned. In all of the cases the spectrum of positron lifetime was distributed into three components, with the long-life component ranging from 1.8 to 2.08 ns and the intensity taking on values from 18 to 24%. Making use of Tao–Eldrup model, the average radius of the free volume, in which o-Ps annihilated, and the degree of filling in the volume were determined. It was found that the value of the long-life component for human insulin is higher than that of animal insulin. Moreover, the value of this component clearly…
Physicochemical stability of human insulin 1 I.U./mL infusion solution in 50 mL polypropylene syringes
2021
Abstract Objectives The objective of this study was to investigate the physicochemical stability of human insulin 1 I.U./mL injection solutions (Insuman® Rapid) diluted with 0.9% NaCl solution in 50 mL disposable three-piece polypropylene syringes and stored refrigerated or at room temperature. Methods 1 I.U./mL test solutions were prepared with Insuman® Rapid and 0.9% sodium chloride infusion solution in 50 mL Original-Perfusor® syringes and BD® Perfusion syringes. Test solutions were stored for 90 days at 2–8 °C/dark or 48 h at 20–25 °C/diffuse room light in order to determine chemical stability. Additional test solutions were stored 28 days at 2–8 °C/dark followed by 24 h at 20–25 °C/dif…
Corrigendum to “Kinetics of Different Processes in Human Insulin Amyloid Formation” [J. Mol. Biol. 366/1 (2007) 258-274]
2011
Mauro Manno⁎, Emanuela Fabiola Craparo, Alessandro Podesta, Donatella Bulone, Rita Carrotta, Vincenzo Martorana, Guido Tiana and Pier Luigi San Biagio Institute of Biophysics at Palermo Italian National Research Council, via U. La Malfa 153, I-90146 Palermo, Italy Dipartimento di Chimica e Tecnologie Farmaceutiche Universita di Palermo via Archirafi 32 I-90123 Palermo, Italy Department of Physics and CIMAINA, University of Milano, via Celoria 16, I-20133 Milano, Italy Department of Physics, University of Milano and INFN, via Celoria 16, I-20133 Milano, Italy
Probing ensemble polymorphism and single aggregate structural heterogeneity in insulin amyloid self-assembly.
2020
Ensembles of protein aggregates are characterized by a nano- and micro-scale heterogeneity of the species. This diversity translates into a variety of effects that protein aggregates may have in biological systems, both in connection to neurodegenerative diseases and immunogenic risk of protein drug products. Moreover, this naturally occurring variety offers unique opportunities in the field of protein-based biomaterials. In the above-mentioned fields, the isolation and structural analysis of the different amyloid types within the same ensemble remain a priority, still representing a significant experimental challenge. Here we address such complexity in the case of insulin for its relevance…