A New Method for the Detection of Racemization during Peptide Synthesis: Stereoselective hydrolysis of diastereomeric peptides by leucine aminopeptidase

1973 ◽  
Vol 56 (2) ◽  
pp. 717-723 ◽  
Author(s):  
Hans Rudolf Bonsshard ◽  
Israel Schechter ◽  
Arieh Berger
2020 ◽  
Vol 84 ◽  
pp. 127-140
Author(s):  
BM Gaas ◽  
JW Ammerman

Leucine aminopeptidase (LAP) is one of the enzymes involved in the hydrolysis of peptides, and is sometimes used to indicate potential nitrogen limitation in microbes. Small-scale variability has the potential to confound interpretation of underlying patterns in LAP activity in time or space. An automated flow-injection analysis instrument was used to address the small-scale variability of LAP activity within contiguous regions of the Hudson River plume (New Jersey, USA). LAP activity had a coefficient of variation (CV) of ca. 0.5 with occasional values above 1.0. The mean CVs for other biological parameters—chlorophyll fluorescence and nitrate concentration—were similar, and were much lower for salinity. LAP activity changed by an average of 35 nmol l-1 h-1 at different salinities, and variations in LAP activity were higher crossing region boundaries than within a region. Differences in LAP activity were ±100 nmol l-1 h-1 between sequential samples spaced <10 m apart. Variogram analysis indicated an inherent spatial variability of 52 nmol l-1 h-1 throughout the study area. Large changes in LAP activity were often associated with small changes in salinity and chlorophyll fluorescence, and were sensitive to the sampling frequency. This study concludes that LAP measurements in a sample could realistically be expected to range from zero to twice the average, and changes between areas or times should be at least 2-fold to have some degree of confidence that apparent patterns (or lack thereof) in activity are real.


2021 ◽  
pp. 112408
Author(s):  
Elizabeth Undiano ◽  
Susana Chávez ◽  
Pedro Mederos ◽  
Marcela Ayala ◽  
Antonio Monroy-Noyola

1966 ◽  
Vol 19 (8) ◽  
pp. 1511 ◽  
Author(s):  
FHC Stewart

Experiments with various N-acylamino acid 2,4,6-trimethylbenzyl esters have shown that the ester group is cleaved selectively by cold trifluoroacetic acid without affecting benzyloxycarbonyl, formyl, or phthaloyl amino-protecting groups present. The possible value of this selective behaviour in peptide syntheses where the use of alkaline conditions would be detrimental is illustrated by the synthesis of certain dipeptide derivatives.


1991 ◽  
Vol 55 (11) ◽  
pp. 2865-2870
Author(s):  
Satoshi Mitsuda ◽  
Ryohei Komaki ◽  
Hideo Hirohara ◽  
Shigeyasu Nabeshima

AMB Express ◽  
2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Christin Slomka ◽  
Sabilla Zhong ◽  
Anna Fellinger ◽  
Ulrike Engel ◽  
Christoph Syldatk ◽  
...  

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