Cleavage of DNA using plant hemoglobins
(2017) KBKL01 20161Pure and Applied Biochemistry
- Abstract
- Three non-symbiotic hemoglobins (nsHb) have been identified in Beta Vulgaris (sugar beet). These are hexacoordinated Hbs with high oxygen affinity. The spectral properties for one of these, BvHb1.1 was analyzed and its molar absorption coefficients determined. Furthermore, an initial safety analysis was carried out by studying the cleavage of plasmid DNA (pDNA) induced by these proteins. The result shows that nsHbs from sugar beet cleave pDNA similarly to what has been reported for other heme containing proteins. However, they are significantly less reactive towards pDNA than recombinant adult Hb. Some variations were identified between the three proteins regarding their reactivity in the presence of different additives. The class I... (More)
- Three non-symbiotic hemoglobins (nsHb) have been identified in Beta Vulgaris (sugar beet). These are hexacoordinated Hbs with high oxygen affinity. The spectral properties for one of these, BvHb1.1 was analyzed and its molar absorption coefficients determined. Furthermore, an initial safety analysis was carried out by studying the cleavage of plasmid DNA (pDNA) induced by these proteins. The result shows that nsHbs from sugar beet cleave pDNA similarly to what has been reported for other heme containing proteins. However, they are significantly less reactive towards pDNA than recombinant adult Hb. Some variations were identified between the three proteins regarding their reactivity in the presence of different additives. The class I protein, BvHb1.2, show an increase in reactivity in the presence of medium amount of salt or buffer while the class II protein, BvHb2, show a distinct decrease in activity at room temperature (20 °C) compared to body temperature (37 °C). These results, especially in relation to further characterization, will provide new insight on the effects of hexacoordination in Hbs and the potential use of these as oxygen carriers in various applications. (Less)
Please use this url to cite or link to this publication:
http://lup.lub.lu.se/student-papers/record/8928891
- author
- Rosendal, Ebba LU
- supervisor
-
- Nélida Leiva LU
- organization
- course
- KBKL01 20161
- year
- 2017
- type
- M2 - Bachelor Degree
- subject
- keywords
- applied biochemistry, tillämpad biokemi
- language
- English
- id
- 8928891
- date added to LUP
- 2017-12-18 10:36:15
- date last changed
- 2017-12-18 10:36:15
@misc{8928891, abstract = {{Three non-symbiotic hemoglobins (nsHb) have been identified in Beta Vulgaris (sugar beet). These are hexacoordinated Hbs with high oxygen affinity. The spectral properties for one of these, BvHb1.1 was analyzed and its molar absorption coefficients determined. Furthermore, an initial safety analysis was carried out by studying the cleavage of plasmid DNA (pDNA) induced by these proteins. The result shows that nsHbs from sugar beet cleave pDNA similarly to what has been reported for other heme containing proteins. However, they are significantly less reactive towards pDNA than recombinant adult Hb. Some variations were identified between the three proteins regarding their reactivity in the presence of different additives. The class I protein, BvHb1.2, show an increase in reactivity in the presence of medium amount of salt or buffer while the class II protein, BvHb2, show a distinct decrease in activity at room temperature (20 °C) compared to body temperature (37 °C). These results, especially in relation to further characterization, will provide new insight on the effects of hexacoordination in Hbs and the potential use of these as oxygen carriers in various applications.}}, author = {{Rosendal, Ebba}}, language = {{eng}}, note = {{Student Paper}}, title = {{Cleavage of DNA using plant hemoglobins}}, year = {{2017}}, }