scholarly journals ISOLATION AND PURIFICATION OF PROTEIN THAT IS IMMUNOLOGICALLY SIMILAR TO HUMAN LACTOFERRIN

2021 ◽  
Vol 11 (2) ◽  
pp. 19-12
Author(s):  
Oksana Boiko ◽  
Aleksandr Nikolaev ◽  
Daria Kozak ◽  
Natalia Gudinskaya ◽  
Maxim Saharov ◽  
...  

The study aimed at isolating a substance that is immunologically similar to human lactoferrin, hereinafter — microbial-derived lactoferrin (MdLF) isolated from K.pneumoniae liquid culture. Protein extraction started with isolation of ballast proteins in 2M ammonium sulphate (p.a.). Ion chromatography with cation-exchange agents was the basic method used for isolating MLF. Proteins from the isolated protein fractions were identified with AGID method. The isolated MLF is glucoprotein with the molecular mass of about 84,000, the agarose diffusion coefficient of 3.1 × 10–7 cm2 sec–1 and the relative electrophoretic mobility of 0.42. MLF is characterized by low hydrophobicity and elutes from phenylSepharose with 0.4 ammonium sulphate. Its isoelectric point equals to 9.2.

Author(s):  
J. S. Chin

A practical engineering calculation method has been formulated for commercial multicomponent fuel stagnant droplet evaporation with variable finite mass and thermal diffusivity. Instead of solving the transient liquid phase mass and heat transfer partial differential equation set, a totally different approach is used. With zero or infinite mass diffusion resistance in liquid phase, it is possible to obtain vapor pressure and vapor molecular mass based on the distillation curve of these turbine fuels. It is determined that Peclet number (Pef) is a suitable parameter to represent the mass diffusion resistance in liquid phase. The vapor pressure and vapor molecular mass at constant finite Pef is expressed as a function of finite Pef, vapor pressure, and molecular mass at zero Pef and infinite Pef. At any time step, with variable finite Pef, the above equation is still valid, and PFsPef=∞, PFsPef=0, MfvPef=∞, MfvPef=0 are calculated from PFsPef≡∞, PFsPef≡0, MfvPef≡∞, MfvPef≡0, thus PFs and Mfv can be determined in a global way which eventually is based on the distillation curve of fuel. The explicit solution of transient heat transfer equation is used to have droplet surface temperature and droplet average temperature as a function of surface Nusselt number and non-dimensional time. The effect of varying com position of multi-component fuel evaporation is taken into account by expressing the properties as a function of molecular mass, acentric factor, critical temperature, and critical pressure. A specific calculation method is developed for liquid fuel diffusion coefficient, also special care is taken to calculate the binary diffusion coefficient of fuel vapor-air in gaseous phase. The effect of Stefan flow and natural convection has been included. The predictions from the present evaporation model for different turbine fuels under very wide temperature ranges have been compared with experimental data with good agreement.


1998 ◽  
Vol 814 (1-2) ◽  
pp. 83-95 ◽  
Author(s):  
Abhinav A Shukla ◽  
Kristopher A Barnthouse ◽  
Sung Su Bae ◽  
J.A Moore ◽  
Steven M Cramer

1999 ◽  
Vol 45 (1) ◽  
pp. 23-30
Author(s):  
Somchai Santiwatanakul ◽  
Noel R Krieg

Autolytic activity in the soluble and sediment fractions of sonicates of the spiral and the coccoid form of Campylobacter upsaliensis could not be demonstrated by native (nondenaturing) polyacrylamide gel electrophoresis (PAGE). Autolysins were detected, however, by using denaturing sodium dodecyl sulfate (SDS) - PAGE gels containing either purified Escherichia coli peptidoglycan or whole cells of Micrococcus luteus (Micrococcus lysodeikticus) as the turbid substrate, with subsequent renaturation by treatment with Triton X-100 buffer. In renaturing gels that contained Escherichia coli peptidoglycan, 14 putative autolytic bands ranging from 200 to 12 kDa were detected. In similar gels containing whole cells of M. luteus, only a single band appeared with a molecular mass of 34 kDa. This band corresponded to one of the bands present in the gels containing Escherichia coli peptidoglycan. This common autolysin was isolated by adsorbing it from Campylobacter upsaliensis soluble fractions onto M. luteus cells and then subjecting these cells to renaturing SDS-PAGE in gels containing Escherichia coli peptidoglycan. The 34-kDa autolysin differed from a single 51-kDa autolysin unique to the M. luteus cells, and when isolated from an SDS-PAGE gel, was pure when tested by isoelectric focusing. The N-terminal amino acid sequence analysis showed the first 15 amino acids of the 34-kDa autolysin to have 67% identity to a part of antigenic protein PEB4 of Campylobacter jejuni. The purified autolysin was used to immunize rabbits and the antibodies produced precipitated autolytic activity from cell lysates. The specificity of the antibodies was shown by Western blotting: only a single specific band occurred, with a molecular mass of 34 kDa, and thus it seems unlikely that the 34-kDa autolysin was derived from any of the other autolysins that were detected.Key words: autolysin, Campylobacter upsaliensis, zymogram, murein hydrolase.


1988 ◽  
Vol 122 (1) ◽  
pp. 43-50 ◽  
Author(s):  
M. A. Chaudry ◽  
Noor-Ul-Islam ◽  
z. Yasin

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