Calculation of injection forces for highly concentrated protein solutions

2015 ◽  
Vol 493 (1-2) ◽  
pp. 70-74 ◽  
Author(s):  
Ingo Fischer ◽  
Astrid Schmidt ◽  
Andrew Bryant ◽  
Ahmed Besheer
Keyword(s):  
Protein Solutions ◽  
Injection Forces

scholarly journals A microfluidic approach to studying the injection flow of concentrated albumin solutions

2021 ◽  
Vol 3 (9) ◽  
Author(s):  
Alfredo Lanzaro
Keyword(s):  
Extensional Viscosity ◽  
Protein Solutions ◽  
List Type ◽  
High Concentration ◽  
Complex Flow ◽  
Injection Process ◽  
Injection Flow ◽  
On Chip ◽  
Injection Force ◽  
Injection Forces

Abstract Subcutaneous injection by means of prefilled syringes allows patients to self-administrate high-concentration (100 g/L or more) protein-based drugs. Although the shear flow of concentrated globulins or monoclonal antibodies has been intensively studied and related to the injection force proper of SC processes, very small attention has been paid to the extensional behavior of this category of complex fluids. This work focuses on the flow of concentrated bovine serum albumin (BSA) solutions through a microfluidic “syringe-on-chip” contraction device which shares some similarities with the geometry of syringes used in SC self-injection. By comparing the velocity and pressure measurements in complex flow with rheometric shear measurements obtained by means of the “Rheo-chip” device, it is shown that the extensional viscosity plays an important role in the injection process of protinaceous drugs. Article Highlights A microfluidic “syringe on chip” device mimicking the injection flow of protinaceous drugs has been developed. The velocity field of concentrated BSA solutions through the “syringe on chip” is Newtonian-like. The extensional viscosity of concentrated protein solutions should also be considered when computing injection forces through needles.

Characterization of frozen hydrated biological specimens by low-loss EELS

1992 ◽  
Vol 50 (2) ◽  
pp. 1572-1573
Author(s):  
Songquan Sun ◽  
Richard D. Leapman
Keyword(s):  
Water Content ◽  
Direct Method ◽  
Internal Standard ◽  
Dry Weight ◽  
Dark Field ◽  
Protein Solutions ◽  
Subcellular Compartment ◽  
Differential Shrinkage ◽  
Electron Energy Loss

Analyses of ultrathin cryosections are generally performed after freeze-drying because the presence of water renders the specimens highly susceptible to radiation damage. The water content of a subcellular compartment is an important quantity that must be known, for example, to convert the dry weight concentrations of ions to the physiologically more relevant molar concentrations. Water content can be determined indirectly from dark-field mass measurements provided that there is no differential shrinkage between compartments and that there exists a suitable internal standard. The potential advantage of a more direct method for measuring water has led us to explore the use of electron energy loss spectroscopy (EELS) for characterizing biological specimens in their frozen hydrated state.We have obtained preliminary EELS measurements from pure amorphous ice and from cryosectioned frozen protein solutions. The specimens were cryotransfered into a VG-HB501 field-emission STEM equipped with a 666 Gatan parallel-detection spectrometer and analyzed at approximately −160 C.

scholarly journals THE REFRACTIVITY OF PROTEIN SOLUTIONS

1935 ◽  
Vol 108 (3) ◽  
pp. 703-707
Author(s):  
David B. Hand
Keyword(s):  
Protein Solutions

scholarly journals The Different Colors of mAbs in Solution

Antibodies ◽  
2021 ◽  
Vol 10 (2) ◽  
pp. 21
Author(s):  
Alexandre Ambrogelly
Keyword(s):  
Visual Inspection ◽  
Quantitative Methods ◽  
Geographical Area ◽  
Therapeutic Protein ◽  
Protein Solutions ◽  
Protein Solution ◽  
Critical Quality Attribute ◽  
Recombinant Therapeutic Protein ◽  
Protein Variants ◽  
Antibody Solution

The color of a therapeutic monoclonal antibody solution is a critical quality attribute. Consistency of color is typically assessed at time of release and during stability studies against preset criteria for late stage clinical and commercial products. A therapeutic protein solution’s color may be determined by visual inspection or by more quantitative methods as per the different geographical area compendia. The nature and intensity of the color of a therapeutic protein solution is typically determined relative to calibrated standards. This review covers the analytical methodologies used for determining the color of a protein solution and presents an overview of protein variants and impurities known to contribute to colored recombinant therapeutic protein solutions.

scholarly journals The crystallization enthalpy and entropy of protein solutions: microcalorimetry, van't Hoff determination and linearized Poisson–Boltzmann model of tetragonal lysozyme crystals

2021 ◽  
Vol 23 (4) ◽  
pp. 2686-2696
Author(s):  
Lorena Hentschel ◽  
Jan Hansen ◽  
Stefan U. Egelhaaf ◽  
Florian Platten
Keyword(s):  
Theoretical Description ◽  
Protein Solutions ◽  
Consistent Picture ◽  
Poisson Boltzmann ◽  
Enthalpy And Entropy ◽  
Boltzmann Model ◽  
Lysozyme Crystals ◽  
Solution Parameters

Microcalorimetric and van't Hoff determinations as well as a theoretical description provide a consistent picture of the crystallization enthalpy and entropy of protein solutions and their dependence on physicochemical solution parameters.

scholarly journals Nuclear Magnetic Relaxation Dispersion in Protein Solutions

1970 ◽  
Vol 245 (17) ◽  
pp. 4251-4255
Author(s):  
Bruce P. Gaber ◽  
Walter E. Schillinger ◽  
Seymour H. Koenig ◽  
Philip Aisen
Keyword(s):  
Magnetic Relaxation ◽  
Nuclear Magnetic Relaxation ◽  
Relaxation Dispersion ◽  
Protein Solutions ◽  
Nuclear Magnetic Relaxation Dispersion ◽  
Nuclear Magnetic

scholarly journals THE ESTIMATION OF ACTIVE NATIVE TRYPSIN IN THE PRESENCE OF INACTIVE DENATURED TRYPSIN

1933 ◽  
Vol 17 (2) ◽  
pp. 159-164 ◽  
Author(s):  
M. L. Anson ◽  
A. E. Mirsky
Keyword(s):  
Protein Solutions ◽  
Digestion Mixture ◽  
Tryptic Activity

Inactive denatured trypsin changes into active native trypsin in the protein solutions which have been used to estimate tryptic activity. If the digestion mixture, however, is alkaline enough and contains enough urea this change does not take place. Such a digestion mixture can be used to estimate active native trypsin in the presence of inactive denatured trypsin.

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