The residual amide content of cellulose sequentially solvent-exchanged and then vacuum-dried

Cellulose ◽  
2008 ◽  
Vol 15 (4) ◽  
pp. 547-553 ◽  
Author(s):  
Daisuke Ishii ◽  
Akira Isogai
Keyword(s):  
Amide Content

Influence of Aqueous Mixtures of Amides on the Kinetics of Electro Reduction of Ni(II) and Co(II) at d. m. e.

1975 ◽  
Vol 30 (11-12) ◽  
pp. 859-861 ◽  
Author(s):  
S. K. Jha ◽  
S. Jha ◽  
S. N. and
Keyword(s):  
Rate Constants ◽  
Electrode Potential ◽  
Gradual Decrease ◽  
Electrode Kinetics ◽  
Aqueous Mixtures ◽  
Aqueous Mixture ◽  
Kinetics Of ◽  
Remarkable Agreement ◽  
Amide Content

Electroreduction of Ni(II) and Co(II) has been carried out in aqueous mixtures of formamide, acetamide and urea. Electrode kinetics in terms of theories of irreversible waves have been studied. After calculating the rate constants by DELAHAY1 and Kou-TECKY2 treatments separately their variation with electrode potential has been used to calculate the product ‘ana’. The rate constants and ‘ana’ calculated from two different approaches show remarkable agreement. `ana’ records a gradual decrease with increasing amide content of the aqueous mixture.

Effect of zinc dificiency stages on the amide content of tomato plants

1964 ◽  
Vol 51 (19) ◽  
pp. 468-468 ◽  
Author(s):  
E. Vrachnou ◽  
C. Dassiou ◽  
A. Pomoni
Keyword(s):  
Tomato Plants ◽  
Amide Content

scholarly journals Chemical differences between thyrotropin isohormones

1977 ◽  
Vol 167 (1) ◽  
pp. 279-280 ◽  
Author(s):  
K M M Davy ◽  
J S Fawcett ◽  
C J O R Morris
Keyword(s):  
Electrochemical Properties ◽  
Isoelectric Focusing ◽  
Amide Content

Amide determinations have been carried out, with a newly developed g.l.c. method, on thyrotropin hormones prepared by isoelectric focusing. The observed differences in amide content fully account for the differences in the electrochemical properties of the isohormones.

The Action of Periodic Acid and its Salts on Wool

1969 ◽  
Vol 39 (9) ◽  
pp. 858-865 ◽  
Author(s):  
A. Kantouch ◽  
A. Bendak
Keyword(s):  
Free Amino ◽  
Binding Capacity ◽  
Periodic Acid ◽  
Periodate Oxidation ◽  
Oxidation Products ◽  
Amino Groups ◽  
Periodate Treatment ◽  
Aldehyde Oxidation ◽  
Sulfur Containing ◽  
Amide Content

Sulfur and nitrogen of periodate-oxidized wool as well as resulting oxidation compounds were investigated. It was found that sulfur content decreased gradually with oxidation. The greatest part of this decrease was found in solution either as sulfuric acid or as sulfur-containing proteinic products. Nitrogen content of wool is nearly unaffected by periodate treatment. Aldehyde oxidation products condense with amino groups of wool, as indicated by infrared spectroscopy. The acid-binding capacity of periodate-treated wool decreased with oxidation, most probably because of the blocking of free amino groups. The amide content as well as the base-binding capacity increase with oxidation. A reaction mechanism for periodate oxidation with wool is suggested.

scholarly journals The isolation and characterization of corticotropin from the pituitary gland of the ostrich Struthio camelus

1977 ◽  
Vol 165 (3) ◽  
pp. 519-523 ◽  
Author(s):  
R J Naudé ◽  
W Oelofsen
Keyword(s):  
Amino Acid ◽  
Polyacrylamide Gel Electrophoresis ◽  
Amino Acid Residues ◽  
Struthio Camelus ◽  
Isolation And Characterization ◽  
Isoelectric Points ◽  
Pituitary Glands ◽  
Amide Content

1. Avian corticotropin (ACTH) was purified from both fresh and aged pituitary glands of the ostrich Struthio camelus. 2. The isolation of corticotropin in pure form involved acid/acetone extraction, NaCl fractionation, CM-cellulose chromatography and Sephadex G-50 chromatography. 3. The hormone preparations from fresh and aged glands behaved as single substances on polyacrylamide-gel electrophoresis, and both preparations were found to consist of 39 amino acid residues, in identical molar proportions for the different amino acids. 4. The isoelectric points of the two hormone preparations were estimated to be in the range pH 8.3-8.7, indicating possible differences in amide content, and the N-terminal amino acid of both preparations appeared to be serine. 5. The hormone preparations from fresh and aged glands exhibited similar biological potencies (73 and 77 i.u./mg respectively), as measured by steroidogenesis in vitro. 6. Apart from possible differences in amide content, the corticotropin preparations obtained from fresh and aged glands appear to be indistinguishable.

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