The Study of Alanine Transaminase Activity in Tissues of Silkworm ( Bombyx mori ) via Direct Analysis in Real-Time (DART) Mass Spectrometry

Alanine transaminase (ALT) is an important amino acid-metabolizing enzyme in silkworm L., and is mainly involved in transferring glutamate to alanine (serving as an essential precursor in silk protein synthesis) through transamination. Therefore, it is generally believed that silk protein synthesis...

Full description

Saved in:
Bibliographic Details
Published in:Molecules (Basel, Switzerland) Switzerland), 2023-05, Vol.28 (10), p.4131
Main Authors: Wu, Guohua, Jiang, Lei, Guo, Jianjun, Li, Wushuang, Ma, Lin, Tang, Bozhi, Liu, Charles C
Format: Article
Language:English
Subjects:
Alanine
Alanine transaminase
Alanine Transaminase - metabolism
ALT
Animals
biochemical analysis
Bombyx - chemistry
Bombyx mori
DART-MS
Digestive System - metabolism
Electrodes
Enzymes
Experiments
Fat body
Gases
Hemolymph
Insect Proteins - metabolism
Ion sources
Ions
Mass Spectrometry
Mass spectroscopy
Midgut
Protein biosynthesis
Protein synthesis
Proteins
Quadrupoles
Real time
Reproducibility
Scientific imaging
Silk
Silk - chemistry
Silk gland
Silkworms
Tissues
Trachea
Transaminases
Citations: Items that this one cites
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Alanine transaminase (ALT) is an important amino acid-metabolizing enzyme in silkworm L., and is mainly involved in transferring glutamate to alanine (serving as an essential precursor in silk protein synthesis) through transamination. Therefore, it is generally believed that silk protein synthesis in the silk gland and the cocoon quantity increase with the increase in ALT activity to a certain extent. Here, a novel analytical method was developed to determine the ALT activity in several key tissues of L. including the posterior silk gland, midgut, fat body, middle silk gland, trachea and hemolymph, by combining the direct-analysis-in-real-time (DART) ion source with a triple-quadrupole mass spectrometer. In addition, a traditional ALT activity assay, the Reitman-Frankel method, was also used to measure ALT activity for comparison. The ALT activity results obtained via the DART-MS method are in good agreement with those obtained via the Reitman-Frankel method. However, the present DART-MS method provides a more convenient, rapid and environmentally friendly quantitative method for ALT measurement. Especially, this method can also monitor ALT activity in different tissues of L. in real time.
ISSN:1420-3049
1420-3049
DOI:10.3390/molecules28104131