A type II lectin, designated as DlyL2, was purified from Dioclea
lasiophylla Mart ex Benth seeds and some of its physicochemical
properties determined. The lectin demonstrated specificity for
alpha-lactose and N-acetyl-D-galactosamine and was able to interact with
porcine stomach mucin. DlyL2 has 0.78 % carbohydrates in its
composition, therefore can be considered a glycoprotein. In addition,
its hemagglutinating activity remained stable M a temperature of 90
degrees C and in a pH range from 5 to 10. Metal chelation treatment did
not affect DlyL2 activity suggesting ifs not a metalloprotein. Dly12
showed an apparent mass of 31 kDa and average molecular mass of 26.371
kDa. Primary structure data could be generated from the partial amino
acid sequence of DlyL2, with about 192 residues sequenced by a
combination of Edman degradation and tandem mass spectrometry. The
lectin is similar to other type II lectins from Diocleinae subtribe, as
well as lectins derived from species of more ancient tribes of the
Fabaceae family. In addition, DlyL2 exhibited no toxicity to Anemia sp.
nauplii. The present study expands the knowledge about the specificity,
structural and physicochemical properties of Diocleinae type II lectins.
%0 Journal Article
%1 WOS:000531102600013
%A Cavada, Benildo Sousa
%A Pinto-Junior, Vanir Reis
%A Osterne, Vinicius Jose Silva
%A Lossio, Claudia Figueiredo
%A Silva, Mayara Torquato Lima
%A Correia, Jorge Luis Almeida
%A Correia, Sarah Elizabeth Gomes
%A Nagano, Celso Shiniti
%A Oliveira, Messias Vital
%A Lima, Lara Dias
%A Vital, Ana Paula Moreira Sousa
%A Leal, Rodrigo Bainy
%A Nascimento, Kyria Santiago
%C THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND
%D 2020
%I ELSEVIER SCI LTD
%J PROCESS BIOCHEMISTRY
%K Dioclea Diocleinae} II lasiophylla; lectin; {Type
%P 104-114
%R 10.1016/j.procbio.2020.03.026
%T A Diocleinae type II lectin from Dioclea lasiophylla Mart. Ex Benth
seeds specific to alpha-lactose/GalNAc
%V 93
%X A type II lectin, designated as DlyL2, was purified from Dioclea
lasiophylla Mart ex Benth seeds and some of its physicochemical
properties determined. The lectin demonstrated specificity for
alpha-lactose and N-acetyl-D-galactosamine and was able to interact with
porcine stomach mucin. DlyL2 has 0.78 % carbohydrates in its
composition, therefore can be considered a glycoprotein. In addition,
its hemagglutinating activity remained stable M a temperature of 90
degrees C and in a pH range from 5 to 10. Metal chelation treatment did
not affect DlyL2 activity suggesting ifs not a metalloprotein. Dly12
showed an apparent mass of 31 kDa and average molecular mass of 26.371
kDa. Primary structure data could be generated from the partial amino
acid sequence of DlyL2, with about 192 residues sequenced by a
combination of Edman degradation and tandem mass spectrometry. The
lectin is similar to other type II lectins from Diocleinae subtribe, as
well as lectins derived from species of more ancient tribes of the
Fabaceae family. In addition, DlyL2 exhibited no toxicity to Anemia sp.
nauplii. The present study expands the knowledge about the specificity,
structural and physicochemical properties of Diocleinae type II lectins.
@article{WOS:000531102600013,
abstract = {A type II lectin, designated as DlyL2, was purified from Dioclea
lasiophylla Mart ex Benth seeds and some of its physicochemical
properties determined. The lectin demonstrated specificity for
alpha-lactose and N-acetyl-D-galactosamine and was able to interact with
porcine stomach mucin. DlyL2 has 0.78 % carbohydrates in its
composition, therefore can be considered a glycoprotein. In addition,
its hemagglutinating activity remained stable M a temperature of 90
degrees C and in a pH range from 5 to 10. Metal chelation treatment did
not affect DlyL2 activity suggesting ifs not a metalloprotein. Dly12
showed an apparent mass of 31 kDa and average molecular mass of 26.371
kDa. Primary structure data could be generated from the partial amino
acid sequence of DlyL2, with about 192 residues sequenced by a
combination of Edman degradation and tandem mass spectrometry. The
lectin is similar to other type II lectins from Diocleinae subtribe, as
well as lectins derived from species of more ancient tribes of the
Fabaceae family. In addition, DlyL2 exhibited no toxicity to Anemia sp.
nauplii. The present study expands the knowledge about the specificity,
structural and physicochemical properties of Diocleinae type II lectins.},
added-at = {2022-05-23T20:00:14.000+0200},
address = {THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND},
author = {Cavada, Benildo Sousa and Pinto-Junior, Vanir Reis and Osterne, Vinicius Jose Silva and Lossio, Claudia Figueiredo and Silva, Mayara Torquato Lima and Correia, Jorge Luis Almeida and Correia, Sarah Elizabeth Gomes and Nagano, Celso Shiniti and Oliveira, Messias Vital and Lima, Lara Dias and Vital, Ana Paula Moreira Sousa and Leal, Rodrigo Bainy and Nascimento, Kyria Santiago},
biburl = {https://www.bibsonomy.org/bibtex/2bbc2040833f95bd40facecc4b97b4a1b/ppgfis_ufc_br},
doi = {10.1016/j.procbio.2020.03.026},
interhash = {c8cf259bef130a6c7c4e5f37fba28de1},
intrahash = {bbc2040833f95bd40facecc4b97b4a1b},
issn = {1359-5113},
journal = {PROCESS BIOCHEMISTRY},
keywords = {Dioclea Diocleinae} II lasiophylla; lectin; {Type},
pages = {104-114},
publisher = {ELSEVIER SCI LTD},
pubstate = {published},
timestamp = {2022-05-23T20:00:14.000+0200},
title = {A Diocleinae type II lectin from Dioclea lasiophylla Mart. Ex Benth
seeds specific to alpha-lactose/GalNAc},
tppubtype = {article},
volume = 93,
year = 2020
}