Gel electrophoresis bands

The reaction of l-ethyl-3(3-dimethylaminopropyl)carbodi-imide with bovine lutrophin has been studied and the reaction conditions have been investigated. Spectrophotometric measurements, tryptic peptide maps, and sodium dodecyl sulphate-urea polyacrylamide gel electrophoresis banding patterns were obtained and compared for native and cross-linked derivatives of the glycoprotein hormone. ... 

UHMWPE samples were incubated in BSF, and investigated for adsorbed proteins in the range of plasma proteins by means of protein desorption and gel electrophoresis. Bands of adsorbed proteins corresponding to albumin, immunoglobulin heavy chain... 

Fig. 9.3 Dendrogram derived from clustering analysis of denaturating gel electrophoresis banding profile of rumen bacterial 16S rRNA from lambs fed concentrate with (TY) or without (TN) tannins...

Due to the insolubility of AP-aggregates, fibril formation could not be analyzed directly by mass spectrometry. In order to determine the molecular composition of aggregates, in gel tryptic digestion and mass spectrometric analysis of the gel electrophoresis bands of Ap-oligomers was performed. AP(l-40) was subjected to fibril growth at 1 J,g/ jL (220 pM) in buffer solution, pH 7.5, and incubated for 5 days at... 

Slater, GW Tnrmel, C Lalande, M Noolandi, J, DNA Gel Electrophoresis Effect of Eield Intensity and Agarose Concentration on Band Inversion, Biopolymers 28, 1793, 1989. Slattery, J, Elow of Viscoelastic Elnids Throngh Porons Media, AIChE Jonmal 13,1066,1967. Slattery, JC, Momentnm, Energy, and Mass Transfer in Continna Robert E. Krieger Melbourne, EL, 1981. 

SDS gel electrophoresis separation in total denaturing conditions was carried out on the protein of culture filtrates and proteins of known molecular mass. The four dark bands (Figure 2) which appear in the gel between 45 and 36 kDa of the standards were assumed to be PG based on the gel filtration results for PG activity and total protein. The relative molecular mass of the four protein bands were estimated as 45 kDa, 42 kDa, 39 kDa and 36 kDa. It was calculated that about 85% of total protein secreted into the culture medium by K. marxianus consisted of PG. 

Molecular masses of the same enzymes of different species are different. Molecular mass of the laccase of Pleorotus ostreatus was found to be 66.8 kDa by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) [48]. Purified enzyme of T. versicolor having a single band with a molecular mass of 68 kDa was in the same range with the molecular weights of laccase isoforms isolated from 2,5-xylidine-induced cultures of T. versicolor [49]. 

SDS polyacrylamide gel electrophoresis (SDS-PAGE) represents the most commonly used analytical technique in the assessment of final product purity (Figure 7.1). This technique is well established and easy to perform. It provides high-resolution separation of polypeptides on the basis of their molecular mass. Bands containing as little as 100 ng of protein can be visualized by staining the gel with dyes such as Coomassie blue. Subsequent gel analysis by scanning laser densitometry allows quantitative determination of the protein content of each band (thus allowing quantification of protein impurities in the product). 

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