PMID- 3365404
OWN - NLM
STAT- MEDLINE
DCOM- 19880614
LR  - 20190613
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 27
IP  - 5
DP  - 1988 Mar 8
TI  - Energy-transfer studies of the distance between the high-affinity metal binding 
      site and the colchicine and 8-anilino-1-naphthalenesulfonic acid binding sites on 
      calf brain tubulin.
PG  - 1508-14
AB  - The high-affinity metal divalent cation Mg2+, associated with the exchangeable 
      guanosine 5'-triphosphate (GTP) binding site (E site) on purified tubulin, has 
      been replaced by the transition metal ion Co2+ on tubulin as well as on the 
      tubulin-colchicine, tubulin-allocolchicine and 
      tubulin-8-anilino-1-naphthalenesulfonic acid (tubulin-ANS) complexes. While pure 
      native tubulin readily incorporated 0.8 atom of Co2+ per tubulin alpha-beta 
      dimer, incorporation was reduced to 0.4 atom of Co2+ per mole of tubulin when it 
      was complexed with colchicine, indicating that the conformational change induced 
      in tubulin by the binding of colchicine leads to a reduced accessibility of the 
      divalent cation binding site linked to the E site without necessarily changing 
      the intrinsic binding constant. The fluorescence emission spectra of 
      tubulin-bound colchicine, allocolchicine, and ANS displayed a strong overlap with 
      the Co2+ absorption spectrum, identifying these as adequate donor-acceptor pairs. 
      Fluorescence energy-transfer measurements were carried out between tubulin-bound 
      colchicine (or allocolchicine) and ANS as donors and tubulin-complexed Co2+ as 
      acceptor. It was found that the distance between the ANS and the high-affinity 
      divalent cation binding sites is greater than 28 A, while that between the 
      colchicine and the divalent cation binding sites is greater than 24 A.(ABSTRACT 
      TRUNCATED AT 250 WORDS)
FAU - Ward, L D
AU  - Ward LD
AD  - Graduate Department of Biochemistry, Brandeis University, Waltham, Massachusetts 
      02254.
FAU - Timasheff, S N
AU  - Timasheff SN
LA  - eng
GR  - CA-16707/CA/NCI NIH HHS/United States
GR  - GM-14603/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Anilino Naphthalenesulfonates)
RN  - 0 (Fluorescent Dyes)
RN  - 0 (Tubulin)
RN  - 3G0H8C9362 (Cobalt)
RN  - 630I4V6051 (1-anilino-8-naphthalenesulfonate)
SB  - IM
MH  - Anilino Naphthalenesulfonates/*metabolism
MH  - Animals
MH  - Binding Sites
MH  - Brain/metabolism
MH  - Cattle
MH  - Cobalt/*metabolism
MH  - Energy Transfer
MH  - Fluorescent Dyes
MH  - Kinetics
MH  - Protein Binding
MH  - Spectrometry, Fluorescence
MH  - Tubulin/isolation & purification/*metabolism
EDAT- 1988/03/08 00:00
MHDA- 1988/03/08 00:01
CRDT- 1988/03/08 00:00
PHST- 1988/03/08 00:00 [pubmed]
PHST- 1988/03/08 00:01 [medline]
PHST- 1988/03/08 00:00 [entrez]
AID - 10.1021/bi00405a017 [doi]
PST - ppublish
SO  - Biochemistry. 1988 Mar 8;27(5):1508-14. doi: 10.1021/bi00405a017.