Zobrazeno 1 - 3
of 3
pro vyhledávání: '"John D. McVITTIE"'
Publikováno v:
European Journal of Biochemistry. 56:173-182
The self-association of the separate histone fractions isolated from chicken erythrocytes has been studied in solution at a number of different pH values and ionic strengths. The apparent molecular weights of the histones were determined over a range
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d52313c4f279d1347475ed5197a7cd73
https://doi.org/10.1111/j.1432-1033.1975.tb02220.x
https://doi.org/10.1111/j.1432-1033.1975.tb02220.x
Publikováno v:
European Journal of Biochemistry. 29:67-73
A method is described for the purification of the enzyme triosephosphate isomerase from chicken breast muscle. The physical properties are compared with those of triosephosphate isomerase from rabbit muscle. 1 The enzyme prepared from chicken muscle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bf1d0953711d9a20dd9f5bc8280685e0
https://doi.org/10.1111/j.1432-1033.1972.tb01957.x
https://doi.org/10.1111/j.1432-1033.1972.tb01957.x
Publikováno v:
European journal of biochemistry. 81(2)
1. The process of denaturation of the chicken muscle dimeric enzyme triosephosphate isomerase on addition of guanidinium chloride has been studied at pH 7.6, the pH at which the recovery of activity is optimal (100%) on removal of denaturant. Determi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::53f4f8ffc19cb9ecd007c5b29c929888
https://pubmed.ncbi.nlm.nih.gov/598372
https://pubmed.ncbi.nlm.nih.gov/598372