scholarly journals Isolation and Characterization of Nanocellulose Obtained from Industrial Crop Waste Resources by Using Mild Acid Hydrolysis

2018 ◽  
Vol 6 (4) ◽  
pp. 362-369 ◽  
Author(s):  
Galia Moreno ◽  
Karla Ramirez ◽  
Marianelly Esquivel ◽  
Guillermo Jimenez
Keyword(s):  
Acid Hydrolysis ◽  
Mild Acid Hydrolysis ◽  
Isolation And Characterization ◽  
Industrial Crop ◽  
Crop Waste ◽  
Mild Acid

Base-catalyzed Degradations of Carbohydrates. X. Degradation by β-Elimination of Methylated Degraded Leiocarpan A

1975 ◽  
Vol 53 (14) ◽  
pp. 2189-2193 ◽  
Author(s):  
Gerald O. Aspinall ◽  
Atmaram S. Chaudhari
Keyword(s):  
Acetic Anhydride ◽  
Acid Hydrolysis ◽  
Mild Acid Hydrolysis ◽  
Anomeric Configuration ◽  
End Groups ◽  
Mild Acid

Treatment of methylated degraded leiocarpan A with l,5-diazabicyclo[5.4.0]undec-5-ene and acetic anhydride, followed by mild acid hydrolysis and de-O-acetylation, furnishes 3,4,6-tri-O-methyl-D-mannose and 3,4-di-O-methyl-6-O-(2,3,4-tri-O-methyl-β-D-xylopyranosyl)-D-mannose. The characterization of the methylated disaccharide provides evidence for the site of attachment and anomeric configuration of the D-xylopyranose end groups in the parent polysaccharide.

Galactomannans from Brazilian seeds: characterization of the oligosaccharides produced by mild acid hydrolysis

1995 ◽  
Vol 17 (1) ◽  
pp. 13-19 ◽  
Author(s):  
Joana Léa M.S. Ganter ◽  
Alain Heyraud ◽  
Carmen L.O. Petkowicz ◽  
Marguerite Rinaudo ◽  
Fany Reicher
Keyword(s):  
Acid Hydrolysis ◽  
Mild Acid Hydrolysis ◽  
Mild Acid

scholarly journals Partial characterization of the polyisoprenoid carrier of N-acetylglucosamine in Glycine max (soya bean)

1980 ◽  
Vol 190 (2) ◽  
pp. 255-261 ◽  
Author(s):  
C M Chadwick ◽  
D H Northcote
Keyword(s):  
Glycine Max ◽  
Acid Hydrolysis ◽  
Catalytic Hydrogenation ◽  
Soya Bean ◽  
Mild Acid Hydrolysis ◽  
Sephadex Column ◽  
Acidic Lipid ◽  
Dolichyl Phosphate ◽  
Mild Acid

Dolichyl phosphate (C55) and dolichyl phosphate prepared from liver were incubated with an enzyme prepared from soya-bean protoplasts. They both stimulated the transfer of radioactivity from UDP-D-glucose to lipid, but the stimulation was greater with liver dolichyl phosphate. Liver dolichyl phosphate with the soya-bean enzyme stimulated the transfer of radioactivity from UDP-N-acetyl-D-[U-14C]glucosamine to acidic lipid. UDP-D-[U-14C]glucose and UDP-N-acetyl-D-[U-14C]glucosamine were used with the soya-bean enzyme to prepare the glycosylated-acid-lipid acceptor of each sugar. Mild acid hydrolysis revealed that the radioactivity in the lipid glucosylated from UDP-glucose was present exclusively as glucose. That in the lipid glycosylated from UDP-N-acetylglucosamine was present mostly as N-acetylglucosamine. The soya-bean acidic-lipid acceptors of glucose and N-acetylglucosamine were stable to both catalytic hydrogenation and treatment with hot aqueous phenol; they behaved in a similar way as authentic alpha-saturated glucosylated polyisoprenyl phosphates. The soya-bean acidic-lipid acceptors of glucose and N-acetylglucosamine were eluted as deoxycholate complexes from a Sephadex column. In comparison with glucosylated polyisoprenyl phosphates of known size, the patterns of elution indicated that both soya-bean lipids contained a polyisoprenoid chain of 18 isoprene units.

Amino acid sequence of cyanogen bromide fragment CB5 of human hemopexin

1989 ◽  
Vol 54 (3) ◽  
pp. 803-810 ◽  
Author(s):  
Ivan Kluh ◽  
Ladislav Morávek ◽  
Manfred Pavlík
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Acid Hydrolysis ◽  
Cyanogen Bromide ◽  
Polypeptide Chain ◽  
Amino Acid Residues ◽  
Mild Acid Hydrolysis ◽  
Methionine Residue ◽  
Cyanogen Bromide Fragment ◽  
Mild Acid

Cyanogen bromide fragment CB5 represents the region of the polypeptide chain of hemopexin between the fourth and fifth methionine residue (residues 232-352). It contains 120 amino acid residues in the following sequence: Arg-Cys-Ser-Pro-His-Leu-Val-Leu-Ser-Ala-Leu-Thr-Ser-Asp-Asn-His-Gly-Ala-Thr-Tyr-Ala-Phe-Ser-Gly-Thr-His-Tyr-Trp-Arg-Leu-Asp-Thr-Ser-Arg-Asp-Gly-Trp-His-Ser-Trp-Pro-Ile-Ala-His-Gln-Trp-Pro-Gln-Gly-Pro-Ser-Ala-Val-Asp-Ala-Ala-Phe-Ser-Trp-Glu-Glu-Lys-Leu-Tyr-Leu-Val-Gln-Gly-Thr-Gln-Val-Tyr-Val-Phe-Leu-Thr-Lys-Gly-Gly-Tyr-Thr-Leu-Val-Ser-Gly-Tyr-Pro-Lys-Arg-Leu-Glu-Lys-Glu-Val-Gly-Thr-Pro-His-Gly-Ile-Ile-Leu-Asp-Ser-Val-Asp-Ala-Ala-Phe-Ile-Cys-Pro-Gly-Ser-Ser-Arg-Leu-His-Ile-Met. The sequence was derived from the data on peptides prepared by cleavage of fragment CB5 by mild acid hydrolysis, by trypsin and chymotrypsin.

Sign in / Sign up

Export Citation Format

Share Document