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© 2019. This work is licensed under https://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.

Abstract

Based on the method of peptide bond cleavage, there are two groups of serine proteinases: exopeptidases (EC 3.4.11-19) that cleave peptide bonds at the ends of a polypeptide, and endopeptidases or proteinases (EC 3.4.21-99), which cleave internal peptide bonds within the polypeptide chain and are named based on the amino acids that form the catalytic site, e.g., aspartic proteinases, cysteine proteinases, metalloproteinases, serine proteinases, threonine proteinases, and glutamic proteinases [8]. Aspartic proteinases, cysteine proteinases, metalloproteinases, and serine proteinases whose actions ensure the survival, proliferation, and maintenance of the Leishmania spp. life cycle in the host have been described. [...]only the genes LinJ13_V3.0940 and LmjF13.1040 have been related with this function [14]. Since these genes are orthologous to serine proteinases in L.(V.) braziliensis, it is possible that the Lbrm.13.0860 gene has the same function, but this has not yet been confirmed for the gene in chromosome 28. Both the membrane and cytosolic fractions were obtained from 108 promastigotes/mL yielding approximately 0.6 ± 0.02 mg/mL protein, which showed a gelatin-SDS-PAGE profile with major proteinase bands with estimated molecular masses of 43 kDa, 48 kDa, 63 kDa, 99 kDa, and 170 kDa in the cytosolic fraction and 67 kDa, 75 kDa, and 170 kDa in the membrane fraction (Figure 1 inset).

Details

Title
Serine Proteinases in Leishmania (Viannia) braziliensis Promastigotes Have Distinct Subcellular Distributions and Expression
Author
Santos-de-Souza, Raquel; Luzia Monteiro de Castro Côrtes; Karen dos Santos Charret; Cysne-Finkelstein, Léa; Alves, Carlos Roberto; Souza-Silva, Franklin
Publication year
2019
Publication date
2019
Publisher
MDPI AG
ISSN
16616596
e-ISSN
14220067
Source type
Scholarly Journal
Language of publication
English
ProQuest document ID
2333594739
Copyright
© 2019. This work is licensed under https://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.