Fluorodensitometric determination of compounds containing primary amino groups with o-phthalaldehyde after separation by HPTLC

1979 ◽  
Vol 12 (12) ◽  
pp. 779-781 ◽  
Author(s):  
G. Gübitz
Keyword(s):  
Amino Groups ◽  
Primary Amino

scholarly journals The Blocked Amino-Terminal Peptide of Feather Keratin

1971 ◽  
Vol 24 (1) ◽  
pp. 179 ◽  
Author(s):  
IJ O'donnell
Keyword(s):  
Molecular Weight ◽  
Acetic Acid ◽  
Amino Groups ◽  
Amino Terminal ◽  
Acetyl Content ◽  
Electrophoretic Patterns ◽  
Isolation And Characterization ◽  
Primary Amino

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).

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
Keyword(s):  
Colorimetric Determination ◽  
Amino Groups ◽  
Primary Amino

New Method for the Determination of Free Amino Groups in Intact Pure Proteins: Relationship to Available Lysine

1976 ◽  
Vol 59 (6) ◽  
pp. 1251-1254
Author(s):  
James M Purcell ◽  
Daniel J Quimby ◽  
James R Cavanaugh
Keyword(s):  
Bovine Serum Albumin ◽  
Bovine Serum ◽  
Free Amino ◽  
Amino Group ◽  
Amino Groups ◽  
Primary Amino ◽  
Available Lysine ◽  
Β Lactoglobulin ◽  
Group Concentration

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.

Determination of Primary Amino Groups by Reaction Chromatography

1971 ◽  
Vol 4 (5) ◽  
pp. 295-299 ◽  
Author(s):  
H. Edward Mishmash ◽  
Clifton E. Meloan
Keyword(s):  
Amino Groups ◽  
Primary Amino ◽  
Reaction Chromatography

A facile, one-step method for the determination of accessible surface primary amino groups on solid carriers

2012 ◽  
Vol 44 (10) ◽  
pp. 1309-1313 ◽  
Author(s):  
Zhenyuan Qu ◽  
Hong Xu ◽  
Puwen Ning ◽  
Hongchen Gu
Keyword(s):  
Amino Groups ◽  
Step Method ◽  
One Step ◽  
Primary Amino ◽  
Accessible Surface

POLYMERS OF AMINOACETALDEHYDE

1945 ◽  
Vol 23b (4) ◽  
pp. 158-163
Author(s):  
H. H. Richmond ◽  
George F. Wright
Keyword(s):  
Molecular Weight ◽  
Ammonium Chloride ◽  
Ammonium Carbonate ◽  
Hydroxyl Groups ◽  
Molecular Weight Determination ◽  
Amino Groups ◽  
Primary Amino

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.

Determination of primary amino groups by gas chromatography

1962 ◽  
Vol 6 (1) ◽  
pp. 45-49 ◽  
Author(s):  
Erik R. Hoffmann ◽  
Ihor Lysyj
Keyword(s):  
Gas Chromatography ◽  
Amino Groups ◽  
Primary Amino

Measurement of proteolysis in cheese: relationship between phosphotungstic acid-soluble N fraction by Kjeldahl and 2,4,6- trinitrobenzenesulphonic acid-reactive groups in water-soluble N

1994 ◽  
Vol 61 (3) ◽  
pp. 437-440 ◽  
Author(s):  
Yvette Bouton ◽  
Remy Grappin
Keyword(s):  
Amino Acids ◽  
Free Amino Acids ◽  
Free Amino ◽  
Phosphotungstic Acid ◽  
Water Soluble ◽  
Hydroxyl Groups ◽  
Amino Groups ◽  
Reactive Groups ◽  
Primary Amino

Free amino groups produced during cheese ripening are used to indicate the extent of cheese proteolysis. Several studies have shown a high correlation between the level of free amino acids and the flavour of Gouda (Aston et al. 1983) or Comté (Grappin & Berdagué, 1989). Measurement of the level of free amino acids seems useful for the investigation of flavour chemistry in cheese (Lemieux et al. 1990). The determination of N fractions is often used to estimate the degree of proteolysis in cheese, but since this procedure is laborious and time consuming several attempts have been made to replace it by more rapid methods (Ardö & Meisel, 1991). Since its introduction by Satake et al. (1960), the 2,4,6-trinitrobenzenesulphonic acid (TNBS) method has been widely used for the determination of free amino groups. Because TNBS does not react with the imino groups of histidine and proline or the hydroxyl groups of tyrosine, serine or threonine, it has been accepted as a selective reagent for primary amino groups (Burger, 1974). Measurement of N by Kjeldahl in the phosphotungstic acid (PTA)–sulphuric acid extract (Gripon et al. 1975) estimates the N of free amino acids and low molecular mass peptides. The purpose of this study was to compare the TNBS and PTA-soluble N methods in order to find out whether the TNBS procedure can replace that of PTA-soluble N in the determination of a cheese proteolysis index.

Two different approaches for developing immunometric assays of haptens

1996 ◽  
Vol 42 (9) ◽  
pp. 1532-1536 ◽  
Author(s):  
J Grassi ◽  
C Créminon ◽  
Y Frobert ◽  
E Etienne ◽  
E Ezan ◽  
...  
Keyword(s):  
Amino Acids ◽  
Monoclonal Antibody ◽  
Solid Phase ◽  
Leukotriene C4 ◽  
Amino Groups ◽  
Small Peptides ◽  
Assay Sensitivity ◽  
Primary Amino ◽  
C And N

Abstract To improve immunoassays of small haptens, we developed two different approaches for their measurement in a non-competitive format. We first devised two-site immunometric assays for small peptides (8-11 amino acids) by selecting two sets of antibodies specifically directed against C- and N-terminal moieties of the peptides. In each case, assay sensitivity improved substantially over that of the corresponding competitive assays. More interestingly, all of these new immunometric assays were much more specific than the competitive assays. In a second approach, we developed a new procedure, solid-phase-immobilized epitope immunoassay (SPIE-IA), in which a single monoclonal antibody uses the same epitope for capture and tracer binding and the hapten is covalently cross-linked to solid-phase proteins. To date, SPIE-IA have been successfully applied to the determination of haptens bearing primary amino groups, including substance P, thyroxine, leukotriene C4, endothelin, and angiotensin II. In each case, assay sensitivity was significantly improved.

Sign in / Sign up

Export Citation Format

Share Document