A non-phosgene process for bioderived polycarbonate with high molecular weight and advanced property profile synthesized using amino acid ionic liquids as catalysts

2020 ◽  
Vol 22 (8) ◽  
pp. 2534-2542 ◽  
Author(s):  
Zhencai Zhang ◽  
Fei Xu ◽  
Yaqin Zhang ◽  
Chenhao Li ◽  
Hongyan He ◽  
...  

Bio-based polycarbonate with high molecular weight and advanced property profile was synthesized using amino acid ionic liquids as catalysts.

1980 ◽  
Vol 192 (2) ◽  
pp. 569-577 ◽  
Author(s):  
J Barr ◽  
P Nordin

Membrane preparations from Acer pseudoplatanus suspension cultures were demonstrated to incorporate radioactivity from GDP-[U-14C]mannose and UDP-N-acetyl-[6-(3)H]glucosamine into high-molecular-weight polymers characterized as glycoprotein. From 20 to 25% of the 14C was incorporated as fucose with the remainder as mannose, whereas 90% of the 3H was incorporated as N-acetylglucosamine with the remainder as N-acetylgalactosamine. Pronase digestion yielded radioactive glycopeptides that were separated into four fractions by gel-permeation chromatography and paper electrophoresis. The isolated glycopeptides differed in molecular weight and isotopes incorporated, as well as in amino-acid and monosaccharide composition. The membrane preparation also incorporated radioactivity from the added nucleotides into chloroform/methanol (2:1, v/v)- and chloroform/methanol/water (10:10:3, by vol.)-soluble lipids, and into an insoluble pellet.


1971 ◽  
Vol 124 (4) ◽  
pp. 759-766 ◽  
Author(s):  
M. R. Redshaw ◽  
B. K. Follett

A single lipophosphoprotein complex, vitellogenin, was isolated and purified from the plasma of oestrogen-stimulated female toads by preparative ultracentrifugation and chromatography on TEAE-cellulose (triethylaminoethylcellulose). The protein contains 12% lipid, 1.5% phosphorus, 1.6% calcium and smaller amounts of carbohydrates and biliverdin. In amino acid composition it is identical with total yolk-platelet protein. The platelet protein, however, is fractionated on TEAE-cellulose into two components, a high-molecular-weight lipovitellin and a smaller phosvitin. Analyses of the soluble plasma vitellogenin suggest that it is a complex of two phosvitin molecules covalently bound to one lipovitellin dimer, and that it is the immediate precursor of the yolk proteins, into which it is converted by a molecular rearrangement. Uptake of vitellogenin from the plasma into the growing oocyte, and its subsequent crystallization as a yolk platelet, appear to be enhanced by gonadotrophic hormones.


1976 ◽  
Vol 73 (3) ◽  
pp. 737-741 ◽  
Author(s):  
J. P. Briand ◽  
K. E. Richards ◽  
J. P. Bouley ◽  
J. Witz ◽  
L. Hirth

1998 ◽  
Vol 180 (2) ◽  
pp. 395-399 ◽  
Author(s):  
Anke Becker ◽  
Alfred Pühler

ABSTRACT The production of the acidic exopolysaccharide succinoglycan (EPS I) by Rhizobium meliloti exoP* mutants expressing an ExoP protein lacking its C-terminal cytoplasmic domain and by mutants characterized by specific amino acid substitutions in the proline-rich motif (RX4PX2PX4SPKX9IXGXMXGXG) located from positions 443 to 476 of the ExoP protein was analyzed. The absence of the C-terminal cytoplasmic ExoP domain (positions 484 to 786) and the substitution of both arginine443 by isoleucine443 and proline457 by serine457 within the proline-rich motif resulted in enhanced production of low-molecular-weight (LMW) EPS I at the expense of high-molecular-weight (HMW) EPS I. The ratios of HMW to LMW EPS I of the wild type and mutant strains increased with osmolarity.


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