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Cleavage of DNA using plant hemoglobins

Rosendal, Ebba LU (2017) KBKL01 20161
Pure 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)
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author
Rosendal, Ebba LU
supervisor
organization
course
KBKL01 20161
year
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},
  keyword      = {applied biochemistry,tillämpad biokemi},
  language     = {eng},
  note         = {Student Paper},
  title        = {Cleavage of DNA using plant hemoglobins},
  year         = {2017},
}