Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Silvia Solís-Mendiola"'
Autor:
Fancisco Javier Tzompantzi Morales, Maximiliano Joel Asomoza Palacios, Jin An Wang, Ulises Arellano Sánchez, Li Fang Chen, Dolores Silvia Solís Mendiola
Publikováno v:
Journal of Materials Science and Engineering A. 7
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a8f53c65e876a68fecb7ba761e776ec8
https://doi.org/10.17265/2161-6213/2017.9-10.003
https://doi.org/10.17265/2161-6213/2017.9-10.003
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1203:121-125
Differential scanning calorimetry (DSC) was employed to study the thermal unfolding of chymopapain (EC 3.4.22.6) and papain (EC 3.4.22.2), two highly homologous cysteine proteinases from Carica papaya. Under all pH conditions used, both enzymes showe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46fc4e83b1e2938107f367a139081db9
https://doi.org/10.1016/0167-4838(93)90045-s
https://doi.org/10.1016/0167-4838(93)90045-s
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1118:288-292
Two forms of proteinase omega were isolated from a commercial preparation of chymopapain (EC 3.4.22.6) by means of cation-exchange liquid chromatography. Their circular dichroism (CD) spectra in the 182-320 nm region indicated that the two forms poss
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::243b20f8148c5b71d98d179fbeedebdc
https://doi.org/10.1016/0167-4838(92)90286-m
https://doi.org/10.1016/0167-4838(92)90286-m
Autor:
Andrés Hernández-Arana, Silvia Solís-Mendiola, Leticia López-Arenas, Jaqueline Padilla-Zúñiga
Publikováno v:
Biochimica et biophysica acta. 1764(7)
We studied the effect of three electrolytes (LiCl, Na(2)SO(4), GuHCl) on the unfolding reaction of chymopapain, a two-domain protein belonging in the papain family of cysteine proteinases. Due to methodological reasons, these studies were carried out
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac90160e96acab94d39384c0c5c050cf
https://pubmed.ncbi.nlm.nih.gov/16837256
https://pubmed.ncbi.nlm.nih.gov/16837256
Publikováno v:
Biochemistry. 38(48)
The thermal denaturation of caricain (the most alkaline of papain-related proteinases) was studied in acid media. Under all conditions tested, caricain denatured irreversibly following a single first-order reaction that involves simultaneous loss of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::860ee21baf11415cf38530286b5e5af6
https://pubmed.ncbi.nlm.nih.gov/10625460
https://pubmed.ncbi.nlm.nih.gov/10625460
Autor:
Luis H. Gutiérrez-González, Jacqueline Padilla-Zúñiga, Arturo Rojo-Domínguez, Silvia Solís-Mendiola, Andrés Hernández-Arana, Alfonso Arroyo-Reyna
Publikováno v:
Biochimica et biophysica acta. 1388(2)
We studied the irreversible thermal denaturation of chymopapain, a papain-related cysteine proteinase. It was found that this process follows simple first-order kinetics under all conditions tested. Rate constants determined by monitoring ellipticity
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04583442bc1acc1fd30eb3139efa8e71
https://pubmed.ncbi.nlm.nih.gov/9858767
https://pubmed.ncbi.nlm.nih.gov/9858767
Publikováno v:
Scopus-Elsevier
Four chymopapain forms were isolated by high-resolution liquid chromatography on a cation-exchange column. The three major forms possess nearly identical secondary and tertiary structures, as judged from their c.d. spectra; these components showed si
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45ac5f48fab6b8c2702b61102bda412d
http://www.scopus.com/inward/record.url?eid=2-s2.0-0024528024&partnerID=MN8TOARS
http://www.scopus.com/inward/record.url?eid=2-s2.0-0024528024&partnerID=MN8TOARS
