TY - JOUR
T1 - Identification and purification of a calcium-binding protein from Bacillus subtilis
AU - Tozzi, Maria Grazia
AU - D'Arcangelo, Ugo
AU - Del Corso, Antonella
AU - Ordal, George W.
N1 - Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1991/10/25
Y1 - 1991/10/25
N2 - A Ca2+-binding protein was identified in Bacillus subtilis in the log phase of growth. The molecular mass of this protein is about 38 kDa as estimated by polyacrylamide gel electrophoresis in the presence of SDS and by gel filtration. The protein was found to be resistant 10 min at 65°C and was purified about 400 times, starting from heated crude extract, by conventional procedures. This novel protein is able to bind Ca2+ in the presence of an excess of MgCl2 and KCl both in solution and after SDS gel electrophoresis and electrotransfer. Since an impairment of the Ca2+ intake, in Bacillus subtilis, results in an impairment of chemotactic behavior (Matsushita, T. et al (1988) FEBS lett. 236, 437-440), 38 kDa protein may be involved in the regulation of chemotaxis.
AB - A Ca2+-binding protein was identified in Bacillus subtilis in the log phase of growth. The molecular mass of this protein is about 38 kDa as estimated by polyacrylamide gel electrophoresis in the presence of SDS and by gel filtration. The protein was found to be resistant 10 min at 65°C and was purified about 400 times, starting from heated crude extract, by conventional procedures. This novel protein is able to bind Ca2+ in the presence of an excess of MgCl2 and KCl both in solution and after SDS gel electrophoresis and electrotransfer. Since an impairment of the Ca2+ intake, in Bacillus subtilis, results in an impairment of chemotactic behavior (Matsushita, T. et al (1988) FEBS lett. 236, 437-440), 38 kDa protein may be involved in the regulation of chemotaxis.
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U2 - 10.1016/0167-4838(91)90144-O
DO - 10.1016/0167-4838(91)90144-O
M3 - Article
C2 - 1932092
AN - SCOPUS:0026008805
VL - 1080
SP - 160
EP - 164
JO - BBA - Protein Structure
JF - BBA - Protein Structure
SN - 1570-9639
IS - 2
ER -