Leucine aminopeptidase activity in mesenterial mast cells of the carp

1959 ◽  
Vol 46 (15) ◽  
pp. 476-477 ◽  
Author(s):  
A. Stolk
Keyword(s):  
Mast Cells ◽  
Leucine Aminopeptidase ◽  
Aminopeptidase Activity

Leucine Aminopeptidase Activity in Mast Cells

Nature ◽  
1959 ◽  
Vol 183 (4653) ◽  
pp. 51-52 ◽  
Author(s):  
O. BRAUN-FALCO ◽  
K. SALFELD
Keyword(s):  
Mast Cells ◽  
Leucine Aminopeptidase ◽  
Aminopeptidase Activity

Quantification of small-scale heterogeneity in aquatic aminopeptidase activity

2020 ◽  
Vol 84 ◽  
pp. 127-140
Author(s):  
BM Gaas ◽  
JW Ammerman
Keyword(s):  
Chlorophyll Fluorescence ◽  
Leucine Aminopeptidase ◽  
Hudson River ◽  
Aminopeptidase Activity ◽  
Small Scale ◽  
Analysis Instrument ◽  
Sequential Samples ◽  
Degree Of Confidence ◽  
The Mean ◽  
Hydrolysis Of

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.

scholarly journals Effect of lead on leucine aminopeptidase activity in human blood.

1980 ◽  
Vol 18 (1) ◽  
pp. 55-57
Author(s):  
Momoko CHIBA ◽  
Kazuko OGIHARA ◽  
Masakazu KIKUCHI
Keyword(s):  
Human Blood ◽  
Leucine Aminopeptidase ◽  
Aminopeptidase Activity

Serum Leucine Aminopeptidase Activity: Clinical and Experimental Studies

Digestion ◽  
1961 ◽  
Vol 95 (1) ◽  
pp. 57-60 ◽  
Author(s):  
P. Braun ◽  
M. Papp ◽  
Eva P. Németh ◽  
I. Horváth
Keyword(s):  
Leucine Aminopeptidase ◽  
Experimental Studies ◽  
Aminopeptidase Activity

A Fluorometric Method for Measuring Leucine Aminopeptidase Activity in Red Blood Cells, Serum, or Tissues

1970 ◽  
Vol 16 (5) ◽  
pp. 412-415 ◽  
Author(s):  
Tetsuo Uete ◽  
Hiroko Tsuchikura ◽  
Kiichi Ninomiya
Keyword(s):  
Blood Cells ◽  
Leucine Aminopeptidase ◽  
Test Sample ◽  
Tissue Homogenate ◽  
Aminopeptidase Activity ◽  
Supernatant Fluid ◽  
Fluorometric Method ◽  
Fluorometric Determination ◽  
Amine Solutions

Abstract A fluorometric determination of leucine aminopeptidase activity in a biological system is described, which is simpler and more sensitive than colori-metric methods. Serum or tissue homogenate is incubated with L-β-naphthylamide at pH 7.2 and 37°C for 10 min. After incubation, ethanol is added to stop the reaction and protein is precipitated. The fluorescence of j3-naphthylamine in the supernatant fluid is measured. Since β-naphthylamide reduces the intensity of the fluorescence of s-naphthyl-amine, solutions used in preparing the standard s-naphthylamine curve must have the same concentration of L-leucyl-s-naphthylamide present as in the test sample.

Detection of leucine aminopeptidase activity in serum using surface-enhanced Raman spectroscopy

The Analyst ◽  
2019 ◽  
Vol 144 (4) ◽  
pp. 1394-1400 ◽  
Author(s):  
Dan Guo ◽  
Zhen-Fei Gan ◽  
Lei Jiang ◽  
Mao-Feng Cao ◽  
Fato Tano Patrice ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Leucine Aminopeptidase ◽  
Surface Enhanced Raman Spectroscopy ◽  
Sensitive Detection ◽  
Aminopeptidase Activity ◽  
Specific Reaction ◽  
Surface Enhanced ◽  
Surface Enhanced Raman

A specific reaction-based SERS approach was developed for the selective and sensitive detection of leucine aminopeptidase activity in serum.

Leucine aminopeptidase activity in blood and hemopoietic organs of different Vertebrates

1987 ◽  
Vol 82 (1) ◽  
pp. 83-88 ◽  
Author(s):  
Rosanna Nano ◽  
Paola De Piceis Polver ◽  
Giuseppe Gerzeli
Keyword(s):  
Leucine Aminopeptidase ◽  
Aminopeptidase Activity ◽  
Hemopoietic Organs

scholarly journals Loss of Pseudomonas aeruginosa PhpA Aminopeptidase Activity Results in Increased algDTranscription

2001 ◽  
Vol 183 (15) ◽  
pp. 4674-4679 ◽  
Author(s):  
Samuel C. Woolwine ◽  
April B. Sprinkle ◽  
Daniel J. Wozniak
Keyword(s):  
Escherichia Coli ◽  
Pseudomonas Aeruginosa ◽  
Dna Binding ◽  
Transcription Initiation ◽  
Leucine Aminopeptidase ◽  
Initiation Site ◽  
Aminopeptidase Activity ◽  
Homologous Protein ◽  
Relevant Property

ABSTRACT Inactivation of Pseudomonas aeruginosa phpA, encoding a putative leucine aminopeptidase, results in increased transcription ofalgD. The homologous protein in Escherichia coli, PepA, is multifunctional, possessing independent aminopeptidase and DNA-binding activities. Here we provide in vitro evidence that PhpA is an aminopeptidase and show that this activity is the relevant property with regard to algD expression. This regulation occurred at the previously mapped algDtranscription initiation site and was not due to activation of an alternative promoter.

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