scholarly journals Determination of the molecular mass of hydrolyzed fibroin obtained from natural silk fibroin by spectrophotometry

Author(s):  
Khushnudbek ESHCHANOV ◽  
Muhabbat BALTAYEVA
2018 ◽  
pp. 138-146 ◽  
Author(s):  
Karin Abraham ◽  
Eckhard Flöter

The presence of polysaccharides in cane and beet raw juices causes several negative effects during the sugar manufacture. These are usually mitigated by enzymatic decomposition of dextrans. Such effects not only depend on the content, but also on the molecular mass distribution. This means that the different dextran fractions specifically affect the process. An accurate process control hence requires the most precise knowledge about the existing content and the molecular mass distribution present. A detailed understanding of the specific processing problems and also a targeted enzyme application hence requires the determination of a total dextran content and also its characterization including the differentiation between the different dextran fractions. An accurate analytical tool which equally satisfies industrial applicability is still lacking. To improve on this situation, two new approaches for the determination of dextran were developed and benchmarked against the commonly used and established Haze Method, which is rather inaccurate and also sensitive to molecular mass variation. The two new approaches are both based on polarimetry. These two methods indicate to be superior over the Haze Method with respect two molecular mass variation and hence enable the determination of a broader molecular size range including also low molecular mass dextrans.


1986 ◽  
Vol 239 (3) ◽  
pp. 777-780 ◽  
Author(s):  
C Y Yang ◽  
F S Lee ◽  
L Chan ◽  
D A Sparrow ◽  
J T Sparrow ◽  
...  

Apolipoprotein B-100 (apo B-100) is the protein ligand in low-density lipoproteins that binds to a specific cell-surface receptor. Its molecular mass has been a subject of controversy. We have determined the molecular mass of the protein by a chemical approach. After complete CNBr cleavage, the C-terminal fragment of apo B-100 was purified by reverse-phase h.p.l.c. Amino acid N- and C-terminal analyses confirm that this peptide represents the C-terminal peptide as deduced from the DNA sequence of a human apo B-100 cDNA clone. A chemically synthesized peptide was used to determine the recovery of the peptide (74.72%). On the basis of these data, the molecular mass of apo B-100 was determined to be 496.82 +/- 24.84 kDa.


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