Colorimetric determination of reactive primary amino groups of macro- and microsolid supports

1993 ◽  
Vol 38 (1-2) ◽  
pp. 15-25 ◽  
Author(s):  
Philemon E. Tyllianakis ◽  
Sotiris E. Kakabakos ◽  
Gregory P. Evangelatos ◽  
Dionyssis S. Ithakissios
1971 ◽  
Vol 24 (1) ◽  
pp. 179 ◽  
Author(s):  
IJ O'donnell

Proteins extracted from reduced and carboxymethylated feather keratins (SCM-keratins) have been studied by Harrap and Woods (1964a, 1964b, 1967). They have demonstrated the presence of electrophoretic heterogeneity amongst the proteins and have obtained a molecular weight of approximately 11,000 in agreement with earlier work of Woodin (1954). There was no indication of marked heterogeneity with respect to size. Using acid hydrolysis and determination of acetic acid produced they found an acetyl content of 1 �30 molesj104 g in the rachis off owl feathers. These were thought to be attached to primary amino groups since there were no O-acetyl groups. In the present paper the isolation and characterization of the predominant, and probably sole, amino-terminal tripeptide from goose feather calamus is described. Goose feather calamus was chosen because its extracted proteins had one of the simplest electrophoretic patterns of proteins from the feathers of a number of species (Harrap and Woods 1967).


2010 ◽  
Vol 19 (3) ◽  
pp. 683-689 ◽  
Author(s):  
Luz M. Ramos-Ponce ◽  
Mireille Vega ◽  
Georgina C. Sandoval-Fabián ◽  
Edith Colunga-Urbina ◽  
Nagamani Balagurusamy ◽  
...  

1976 ◽  
Vol 59 (6) ◽  
pp. 1251-1254
Author(s):  
James M Purcell ◽  
Daniel J Quimby ◽  
James R Cavanaugh

Abstract A new rapid method for the quantitative and routine determination of free amino groups in intact pure proteins has been developed. Primary amino groups are labeled with fluorescamine and the labeled groups are detected by absorption spectroscopy in the range 375–390 nm. The amino group concentration can be determined in a few minutes without hydrolyzing the labeled protein and extracting a lysine derivative. The method was tested with the following proteins: lysozyme, α-lactalbumin, β-lactoglobulin, bovine serum albumin, ribonuclease, ribonuclease-S-peptide, and αsl-rasciii B. Application of this method to the estimation of available lysine is discussed.


1971 ◽  
Vol 4 (5) ◽  
pp. 295-299 ◽  
Author(s):  
H. Edward Mishmash ◽  
Clifton E. Meloan

Biomaterials ◽  
1994 ◽  
Vol 15 (4) ◽  
pp. 289-297 ◽  
Author(s):  
S KAKABAKOS ◽  
P TYLLIANAKIS ◽  
G EVANGELATOS ◽  
D ITHAKISSIOS

2012 ◽  
Vol 44 (10) ◽  
pp. 1309-1313 ◽  
Author(s):  
Zhenyuan Qu ◽  
Hong Xu ◽  
Puwen Ning ◽  
Hongchen Gu

1945 ◽  
Vol 23b (4) ◽  
pp. 158-163
Author(s):  
H. H. Richmond ◽  
George F. Wright

The compound designated by Emil Fischer as 2,5-dihydroxypiperazine has been shown to be tris-aminomethyltrioxane by molecular weight determination of its derivatives. These benzoyl and benzenesulphonyl chloride derivatives further demonstrate the absence of hydroxyl groups and the presence of primary amino groups in the original compound. It has been found that use of ammonium carbonate, but not ammonium chloride, enhances the yield of aminoacetal obtained by ammonolysis of chloroacetal.


1962 ◽  
Vol 6 (1) ◽  
pp. 45-49 ◽  
Author(s):  
Erik R. Hoffmann ◽  
Ihor Lysyj

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