{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,7,4]],"date-time":"2025-07-04T10:07:34Z","timestamp":1751623654300},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"3","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1989,9,15]]},"abstract":"<jats:p>Phospholipase A2 (PLA2) from Naja naja atra (Taiwan cobra) snake venom was subjected to lysine modification with trinitrobenzene sulphonic acid (TNBS), and two major trinitrophenylated (TNP) derivatives, TNP-1 and TNP-2, were separated by h.p.l.c. TNP-1 contained only one TNP group on Lys-6 and showed a marked decrease in enzymic activity, but still retained 45% of the lethal toxicity. Both Lys-6 and Lys-65 were modified in TNP-2, and modification of Lys-65 caused a further reduction of the lethal toxicity to 12.6%. However, the antigenicity of both TNP-1 and TNP-2 remained unchanged. The reactivity of Lys-6 and Lys-65 toward TNBS was greatly enhanced by Ca2+ and dihexanoyl-lecithin, suggesting that the two Lys residues are not directly involved in the binding of Ca2+ and substrate. The modified derivatives retained their affinity for Ca2+, indicating that Lys-6 and Lys-65 did not participate in the Ca2+ binding. The TNP derivatives could be regenerated with hydrazine hydrochloride. The biological activities of the regenerated PLA2 are almost the same as those of native PLA2. These results indicate that Lys-6 and Lys-65 are important for the biological activities of PLA2, and incorporation of a bulky TNP group on Lys-6 and Lys-65 might give rise to a distortion of the active conformation of PLA2.<\/jats:p>","DOI":"10.1042\/bj2620855","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T21:14:08Z","timestamp":1439241248000},"page":"855-860","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":22,"title":["Studies on the status of lysine residues in phospholipase A2 from <i>Naja naja atra<\/i> (Taiwan cobra) snake venom"],"prefix":"10.1042","volume":"262","author":[{"given":"C C","family":"Yang","sequence":"first","affiliation":[{"name":"Institute of Life Sciences, National Tsing Hua University, Hsinchu, Taiwan 30043, Republic of China."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"L S","family":"Chang","sequence":"additional","affiliation":[{"name":"Institute of Life Sciences, National Tsing Hua University, Hsinchu, Taiwan 30043, Republic of China."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/262\/3\/855\/596907\/bj2620855.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/262\/3\/855\/596907\/bj2620855.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,25]],"date-time":"2021-11-25T18:14:52Z","timestamp":1637864092000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/262\/3\/855\/25003\/Studies-on-the-status-of-lysine-residues-in"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1989,9,15]]},"references-count":0,"journal-issue":{"issue":"3","published-print":{"date-parts":[[1989,9,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj2620855","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"type":"print","value":"0264-6021"},{"type":"electronic","value":"1470-8728"}],"subject":[],"published":{"date-parts":[[1989,9,15]]}}}