Characterisation of amino acid modified cellulose surfaces using ToF-SIMS and XPS

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 ◽  
...  
Keyword(s):  
Amino Acid ◽  
Tof Sims ◽  
Modified Cellulose

Controlling cell morphology on amino acid-modified cellulose

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 ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cell Morphology ◽  
Modified Cellulose

TOF-SIMS depth profiling of multilayer amino-acid films using large Argon cluster Arn+, C60+and Cs+sputtering ions: A comparative study

2012 ◽  
Vol 45 (1) ◽  
pp. 178-180 ◽  
Author(s):  
N. Wehbe ◽  
T. Tabarrant ◽  
J. Brison ◽  
T. Mouhib ◽  
A. Delcorte ◽  
...  
Keyword(s):  
Amino Acid ◽  
Comparative Study ◽  
Depth Profiling ◽  
Tof Sims ◽  
Sims Depth Profiling

The Mode of Action of Thrombin

1958 ◽  
Vol 02 (03/04) ◽  
pp. 205-217 ◽  
Author(s):  
K Laki ◽  
Jules A. Gladner ◽  
J. E Folk ◽  
D. R Kominz
Keyword(s):  
Amino Acid ◽  
Active Center ◽  
Mode Of Action ◽  
Amino Acid Analysis ◽  
Terminal Amino Acid ◽  
Terminal Amino ◽  
Quantitative Amino Acid Analysis ◽  
Fibrinogen Molecule ◽  
Modified Cellulose

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.

Amino acid modified cellulose whiskers

RSC Advances ◽  
2011 ◽  
Vol 1 (9) ◽  
pp. 1695 ◽  
Author(s):  
Carolina Andreia Cateto ◽  
Arthur Ragauskas
Keyword(s):  
Amino Acid ◽  
Cellulose Whiskers ◽  
Modified Cellulose

Applications of Time-OF-Flight Secondary Ion Mass Spectrometry (TOF-SIMS)

1990 ◽  
Vol 48 (2) ◽  
pp. 308-309
Author(s):  
Bruno Schueler ◽  
Robert W. Odom
Keyword(s):  
Mass Spectrometry ◽  
Secondary Ion Mass Spectrometry ◽  
Structural Information ◽  
Time Of Flight ◽  
Biological Tissues ◽  
Polymer Surfaces ◽  
Tof Sims ◽  
Secondary Ions ◽  
Ion Mass Spectrometry ◽  
Secondary Ion

Time-of-flight secondary ion mass spectrometry (TOF-SIMS) provides unique capabilities for elemental and molecular compositional analysis of a wide variety of surfaces. This relatively new technique is finding increasing applications in analyses concerned with determining the chemical composition of various polymer surfaces, identifying the composition of organic and inorganic residues on surfaces and the localization of molecular or structurally significant secondary ions signals from biological tissues. TOF-SIMS analyses are typically performed under low primary ion dose (static SIMS) conditions and hence the secondary ions formed often contain significant structural information.This paper will present an overview of current TOF-SIMS instrumentation with particular emphasis on the stigmatic imaging ion microscope developed in the authors’ laboratory. This discussion will be followed by a presentation of several useful applications of the technique for the characterization of polymer surfaces and biological tissues specimens. Particular attention in these applications will focus on how the analytical problem impacts the performance requirements of the mass spectrometer and vice-versa.

The staining pattern of the tropomyosin sequence is displayed in a new paracrystal

1986 ◽  
Vol 44 ◽  
pp. 150-151
Author(s):  
M.K. Lamvik ◽  
L.L. Klatt
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Staining Pattern ◽  
Banding Patterns ◽  
Mass Thickness ◽  
New Form

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.

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