TY - JOUR
T1 - The transition metal binding properties of a 3RD generation bleomycin analogue, tallysomycin
AU - Greenaway, Frederick T.
AU - Dabrowiak, James C.
AU - Van Husen, Mark
AU - Grulich, Robert
AU - Crooke, Stanley T.
PY - 1978/12/29
Y1 - 1978/12/29
N2 - Employing a number of physical techniques the transition metal binding site of the bleomycin (BLM) related antibiotic tallysomycin (TLM) has been determined. The new antibiotic was shown to have two metal binding sites. One site is similar to that of bleomycin and involves the pyrimidine-imidazole portion of the molecule. The second binding site, which is thermodynamically less stable than the first site, utilizes the amino group of the L-talose moiety and the amino groups located in the β lysine-spermidine portion of the antibiotic. The presence of two metal binding sites and its implication on the mechanism of action of TLM is also discussed.
AB - Employing a number of physical techniques the transition metal binding site of the bleomycin (BLM) related antibiotic tallysomycin (TLM) has been determined. The new antibiotic was shown to have two metal binding sites. One site is similar to that of bleomycin and involves the pyrimidine-imidazole portion of the molecule. The second binding site, which is thermodynamically less stable than the first site, utilizes the amino group of the L-talose moiety and the amino groups located in the β lysine-spermidine portion of the antibiotic. The presence of two metal binding sites and its implication on the mechanism of action of TLM is also discussed.
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U2 - 10.1016/0006-291X(78)91160-9
DO - 10.1016/0006-291X(78)91160-9
M3 - Article
C2 - 84672
AN - SCOPUS:0018223220
SN - 0006-291X
VL - 85
SP - 1407
EP - 1414
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 4
ER -