{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T03:43:24Z","timestamp":1787024604667,"version":"build-2736575974"},"reference-count":73,"publisher":"Bentham Science Publishers Ltd.","issue":"7","funder":[{"DOI":"10.13039\/501100003141","name":"Conacyt (Mexican Council for Science and Technology) Basic Science","doi-asserted-by":"publisher","award":["18234"],"award-info":[{"award-number":["18234"]}],"id":[{"id":"10.13039\/501100003141","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["eurekaselect.com"],"crossmark-restriction":true},"short-container-title":["PPL"],"published-print":{"date-parts":[[2019,7,22]]},"abstract":"<jats:sec>\n                    <jats:title>Background:<\/jats:title>\n                    <jats:p>Cathepsin D is a lysosomal enzyme that is found in all organisms acting in\nprotein turnover, in humans it is present in some types of carcinomas, and it has a high activity in\nParkinson's disease and a low activity in Alzheimer disease. In marine organisms, most of the\nresearch has been limited to corroborate the presence of this enzyme. It is known that cathepsin D\nof some marine organisms has a low thermostability and that it has the ability to have activity at\nvery acidic pH. Cathepsin D of the Jumbo squid (Dosidicus gigas) hepatopancreas was purified and\npartially characterized. The secondary structure of these enzymes is highly conserved so the role of\ntemperature and pH in the secondary structure and in protein denaturation is of great importance in\nthe study of enzymes. The secondary structure of cathepsin D from jumbo squid hepatopancreas\nwas determined by means of circular dichroism spectroscopy.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Objective:<\/jats:title>\n                    <jats:p>In this article, our purpose was to determine the secondary structure of the enzyme and\nhow it is affected by subjecting it to different temperature and pH conditions.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods:<\/jats:title>\n                    <jats:p>Circular dichroism technique was used to measure the modifications of the secondary\nstructure of cathepsin D when subjected to different treatments. The methodology consisted in\ndissecting the hepatopancreas of squid and freeze drying it. Then a crude extract was prepared by\nmixing 1: 1 hepatopancreas with assay buffer, the purification was in two steps; the first step\nconsisted of using an ultrafiltration membrane with a molecular cut of 50 kDa, and the second step,\na pepstatin agarose resin was used to purification the enzyme. Once the enzyme was purified, the\npurity was corroborated with SDS PAGE electrophoresis, isoelectric point and zymogram. Circular\ndichroism is carried out by placing the sample with a concentration of 0.125 mg \/ mL in a 3 mL\nquartz cell. The results were obtained in mdeg (millidegrees) and transformed to mean ellipticity\nper residue, using 111 g\/mol molecular weight\/residue as average. Secondary-structure estimation\nfrom the far-UV CD spectra was calculated using K2D Dichroweb software.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results:<\/jats:title>\n                    <jats:p>It was found that \u03b1 helix decreases at temperatures above 50 \u00b0C and above pH 4. Heating\nthe enzyme above 70\u00b0C maintains a low percentage of \u03b1 helix and increases \u03b2 sheet. Far-UV CD\nmeasurements of cathepsin D showed irreversible thermal denaturation. The process was strongly\ndependent on the heating rate, accompanied by a process of oligomerization of the protein that\nappears when the sample is heated, and maintained a certain time at this temperature. An amount\ntypically between 3 and 4% \u03b1 helix of their secondary structure remains unchanged. It is consistent\nwith an unfolding process kinetically controlled due to the presence of an irreversible reaction. The\nsecondary structure depends on pH, and a pH above 4 causes \u03b1 helix structures to be modified.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusion:<\/jats:title>\n                    <jats:p>In conclusion, cathepsin D from jumbo squid hepatopancreas showed retaining up to\n4% \u03b1 helix at 80\u00b0C. The thermal denaturation of cathepsin D at pH 3.5 is under kinetic control and\nfollows an irreversible model.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.2174\/0929866526666190405124353","type":"journal-article","created":{"date-parts":[[2019,4,5]],"date-time":"2019-04-05T08:23:28Z","timestamp":1554452608000},"page":"532-541","update-policy":"https:\/\/doi.org\/10.2174\/bsp_crossmark_policy","source":"Crossref","is-referenced-by-count":12,"title":["Effect of Temperature and pH on the Secondary Structure and Denaturation Process of Jumbo Squid Hepatopancreas Cathepsin D."],"prefix":"10.2174","volume":"26","author":[{"given":"Cadena-Cadena","family":"Francisco","sequence":"first","affiliation":[{"name":"Departamento de Investigacion y Posgrado de Alimentos, Universidad de Sonora, Hermosillo, Sonora, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C\u00e1rdenas-L\u00f3pez Jos\u00e9","family":"Luis","sequence":"additional","affiliation":[{"name":"Departamento de Investigacion y Posgrado de Alimentos, Universidad de Sonora, Hermosillo, Sonora, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ezquerra-Brauer Josafat","family":"Marina","sequence":"additional","affiliation":[{"name":"Departamento de Investigacion y Posgrado de Alimentos, Universidad de Sonora, Hermosillo, Sonora, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cinco-Moroyoqui Francisco","family":"Javier","sequence":"additional","affiliation":[{"name":"Departamento de Investigacion y Posgrado de Alimentos, Universidad de Sonora, Hermosillo, Sonora, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"L\u00f3pez-Zavala Alonso","family":"Alexis","sequence":"additional","affiliation":[{"name":"Departamento de Ciencias Quimico Biologicas, Universidad de Sonora, Hermosillo, Sonora, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Santacruz-Ortega Hisila","family":"del Carmen","sequence":"additional","affiliation":[{"name":"Departamento de Investigacion en Pol\u00c3\ufffd\u00c2\u00admeros y Materiales, Universidad de Sonora, Hermosillo, Sonora, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rivero-Espejel Ignacio","family":"Alfredo","sequence":"additional","affiliation":[{"name":"Centro de Graduados e Investigacion en Quimica, Instituto Tecnologico de Tijuana, Tijuana, Baja California, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"965","reference":[{"key":"ref=1","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1042\/bj0740501","volume":"74","author":"Press E.M.","year":"1960","unstructured":"Press EM, Porter RR, Cebra J. 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