Authors:
Humaira Farooqui Department of Biochemistry, Faculty of Science, Jamia Hamdard (Hamdard University), Hamdard Nagar, New Delhi 110062, India
Department of Biotechnology, Faculty of Science, Jamia Hamdard (Hamdard University), Hamdard Nagar, New Delhi 110062, India

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Amena Mahmood Department of Biochemistry, Faculty of Science, Jamia Hamdard (Hamdard University), Hamdard Nagar, New Delhi 110062, India

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Deeba S. Jairajpuri Department of Biochemistry, Faculty of Science, Jamia Hamdard (Hamdard University), Hamdard Nagar, New Delhi 110062, India

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Faizan Ahmad Center for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi 110025, India

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Shakir Ali Department of Biochemistry, Faculty of Science, Jamia Hamdard (Hamdard University), Hamdard Nagar, New Delhi 110062, India

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Abstract

Transition temperature and thermal stability of proteins were studied in the presence and absence of boron. The observed midpoint of thermal denaturation (Tm) of cytochrome c (Cyt c) at pH 9.2 was 68.8 °C, which in the presence of boron increased to 71.0 °C. For metmyoglobin, Tm increased from 79.7 °C in the absence of boron to 83.5 °C in the presence of boron. Boron caused an increase of 10% in the reversibility of thermal denaturation of cytochrome c when compared with control. Activity measurements of the heat treated proteins and Tm suggest an increased thermal stability toward inactivation and denaturation of heme proteins in the presence of boron.

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Journal of Thermal Analysis and Calorimetry
Language English
Size A4
Year of
Foundation
1969
Volumes
per Year
1
Issues
per Year
24
Founder Akadémiai Kiadó
Founder's
Address
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
Publisher Akadémiai Kiadó
Springer Nature Switzerland AG
Publisher's
Address
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
CH-6330 Cham, Switzerland Gewerbestrasse 11.
Responsible
Publisher
Chief Executive Officer, Akadémiai Kiadó
ISSN 1388-6150 (Print)
ISSN 1588-2926 (Online)

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