Amino acid modified cellulose whiskers

RSC Advances ◽  
2011 ◽  
Vol 1 (9) ◽  
pp. 1695 ◽  
Author(s):  
Carolina Andreia Cateto ◽  
Arthur Ragauskas
Soft Matter ◽  
2008 ◽  
Vol 4 (5) ◽  
pp. 1059 ◽  
Author(s):  
Deepak M. Kalaskar ◽  
Julie E. Gough ◽  
Rein V. Ulijn ◽  
William W. Sampson ◽  
David J. Scurr ◽  
...  

Cellulose ◽  
2010 ◽  
Vol 17 (4) ◽  
pp. 747-756 ◽  
Author(s):  
D. M. Kalaskar ◽  
R. V. Ulijn ◽  
J. E. Gough ◽  
M. R. Alexander ◽  
D. J. Scurr ◽  
...  

1958 ◽  
Vol 02 (03/04) ◽  
pp. 205-217 ◽  
Author(s):  
K Laki ◽  
Jules A. Gladner ◽  
J. E Folk ◽  
D. R Kominz

SummaryThe peptides liberated from fibrinogen by the action of thrombin have been isolated on modified cellulose adsorbents. These peptides have been characterized by sedimentation-diffusion measurements by quantitative amino acid analysis, and by C-terminal analysis. Both peptides were found to contain arginine as C-terminal amino acid. Thrombin thus splits specific arginyl-glycine bonds in the fibrinogen molecule. The specificity of thrombin is discussed in view of the finding that the active center of thrombin is similar to that of trypsin and chymotrypsin.


Author(s):  
M.K. Lamvik ◽  
L.L. Klatt

Tropomyosin paracrystals have been used extensively as test specimens and magnification standards due to their clear periodic banding patterns. The paracrystal type discovered by Ohtsuki1 has been of particular interest as a test of unstained specimens because of alternating bands that differ by 50% in mass thickness. While producing specimens of this type, we came across a new paracrystal form. Since this new form displays aligned tropomyosin molecules without the overlaps that are characteristic of the Ohtsuki-type paracrystal, it presents a staining pattern that corresponds to the amino acid sequence of the molecule.


Author(s):  
A. J. Tousimis

The elemental composition of amino acids is similar to that of the major structural components of the epithelial cells of the small intestine and other tissues. Therefore, their subcellular localization and concentration measurements are not possible by x-ray microanalysis. Radioactive isotope labeling: I131-tyrosine, Se75-methionine and S35-methionine have been successfully employed in numerous absorption and transport studies. The latter two have been utilized both in vitro and vivo, with similar results in the hamster and human small intestine. Non-radioactive Selenomethionine, since its absorption/transport behavior is assumed to be the same as that of Se75- methionine and S75-methionine could serve as a compound tracer for this amino acid.


Author(s):  
Chi-Ming Wei ◽  
Margaret Hukee ◽  
Christopher G.A. McGregor ◽  
John C. Burnett

C-type natriuretic peptide (CNP) is a newly identified peptide that is structurally related to atrial (ANP) and brain natriuretic peptide (BNP). CNP exists as a 22-amino acid peptide and like ANP and BNP has a 17-amino acid ring formed by a disulfide bond. Unlike these two previously identified cardiac peptides, CNP lacks the COOH-terminal amino acid extension from the ring structure. ANP, BNP and CNP decrease cardiac preload, but unlike ANP and BNP, CNP is not natriuretic. While ANP and BNP have been localized to the heart, recent investigations have failed to detect CNP mRNA in the myocardium although small concentrations of CNP are detectable in the porcine myocardium. While originally localized to the brain, recent investigations have localized CNP to endothelial cells consistent with a paracrine role for CNP in the control of vascular tone. While CNP has been detected in cardiac tissue by radioimmunoassay, no studies have demonstrated CNP localization in normal human heart by immunoelectron microscopy.


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