5.14 Studies of Spectral Features of Radiation Scattered by Blood …
467
Table 5.5 Ratio of extremums of the amplitude of spectrum of blood absorption to the amount of
protein in a probe at three wavelengths before and after conducting ILBI
Probe No. Experimental group of animals (standard)
Before conducting ILBI
After conducting ILBI
Ratio of amplitude of
extremums of a
spectrum to the
quantity of protein in a
probe at three
wavelengths Ka (1/mg)
Average value
Ka λ i av
Ratio of amplitude of
extremums of a
spectrum to the
quantity of protein in a
probe at three
wavelengths Ka (1/mg)
Average value
Ka λ i av
λ 1
λ 2
λ 3
λ 1
λ 2
λ 3
1
17.08 19.27 16.99 Ka λ1 av
17.8 ± 0.9
20.01 23.48 19.95 Ka λ1 av
19.8 ± 0.9
2
15.99 18.55 15.92 Ka λ2 av
20.4 ± 1.1
17.59 21.24 17.52 Ka λ2 av
23.3 ± 0.9
3
19.85 22.62 19.91 Ka λ3 av
17.8 ± 0.9
20.38 23.29 20/01 Ka λ3 av
17.8 ± 0.9
4
18.52 21.11 18.39
21.66 25.12 21.57
Table 5.6 Difference of the ratio of blood absorption spectra amplitude extremums to the quantity
of protein in the probe Q 1 and Q 2 before and after conducting ILBI
Probe No.
Experimental group of animals (standard)
Before conducting ILBI
After conducting ILBI
Q 1
Q 2
Q 1 av, Q 2 av
Q 1
Q 2
Q 1 av, Q 2 av
1
2.19
2.28
Q 1 av
3.47
3.53
Q 1 av
2
2.56
2.63
2.53 ± 0.14
3.68
3.72
3.46 ± 0.11
3
2.77
2.71
Q 2 av
3.21
3.28
Q 2 av
4
2.60
2.72
2.59 ± 0.12
3.46
3.54
3.52 ± 0.10
Analyzing the derived experimental information from the point of view of possible
mechanism of laser photoactivation of hemoglobin in blood, it is possible to assume
the following: Chromophore hemoglobin group, hem, obviously sustains intramolecular redistribution of electronic levels under the influence of monochromatic radiation
that results in significant enforcement of affinity of porphyrin ring of hem to oxygen.
The studies of blood preparations of a rabbit showed that at ILBI absorption spectra
aspect the changes typical for the oxygenated form of this protein arise.
As far as the influence of laser radiation led to the increase of the level of oxygenation, it can be assumed that the mechanism of photosensitization of reaction of formation of oxyhemoglobin at ILBI is due to intramolecular conformational changes in
the structure of protein part of the hemoglobin molecule along with direct influence
of laser light on the molecule of chromophore (hem).
We should not exclude the fact that the formation of the process of photosensitization of the formation of oxyhemoglobin, and consequently the reaction of oxygen
467
Table 5.5 Ratio of extremums of the amplitude of spectrum of blood absorption to the amount of
protein in a probe at three wavelengths before and after conducting ILBI
Probe No. Experimental group of animals (standard)
Before conducting ILBI
After conducting ILBI
Ratio of amplitude of
extremums of a
spectrum to the
quantity of protein in a
probe at three
wavelengths Ka (1/mg)
Average value
Ka λ i av
Ratio of amplitude of
extremums of a
spectrum to the
quantity of protein in a
probe at three
wavelengths Ka (1/mg)
Average value
Ka λ i av
λ 1
λ 2
λ 3
λ 1
λ 2
λ 3
1
17.08 19.27 16.99 Ka λ1 av
17.8 ± 0.9
20.01 23.48 19.95 Ka λ1 av
19.8 ± 0.9
2
15.99 18.55 15.92 Ka λ2 av
20.4 ± 1.1
17.59 21.24 17.52 Ka λ2 av
23.3 ± 0.9
3
19.85 22.62 19.91 Ka λ3 av
17.8 ± 0.9
20.38 23.29 20/01 Ka λ3 av
17.8 ± 0.9
4
18.52 21.11 18.39
21.66 25.12 21.57
Table 5.6 Difference of the ratio of blood absorption spectra amplitude extremums to the quantity
of protein in the probe Q 1 and Q 2 before and after conducting ILBI
Probe No.
Experimental group of animals (standard)
Before conducting ILBI
After conducting ILBI
Q 1
Q 2
Q 1 av, Q 2 av
Q 1
Q 2
Q 1 av, Q 2 av
1
2.19
2.28
Q 1 av
3.47
3.53
Q 1 av
2
2.56
2.63
2.53 ± 0.14
3.68
3.72
3.46 ± 0.11
3
2.77
2.71
Q 2 av
3.21
3.28
Q 2 av
4
2.60
2.72
2.59 ± 0.12
3.46
3.54
3.52 ± 0.10
Analyzing the derived experimental information from the point of view of possible
mechanism of laser photoactivation of hemoglobin in blood, it is possible to assume
the following: Chromophore hemoglobin group, hem, obviously sustains intramolecular redistribution of electronic levels under the influence of monochromatic radiation
that results in significant enforcement of affinity of porphyrin ring of hem to oxygen.
The studies of blood preparations of a rabbit showed that at ILBI absorption spectra
aspect the changes typical for the oxygenated form of this protein arise.
As far as the influence of laser radiation led to the increase of the level of oxygenation, it can be assumed that the mechanism of photosensitization of reaction of formation of oxyhemoglobin at ILBI is due to intramolecular conformational changes in
the structure of protein part of the hemoglobin molecule along with direct influence
of laser light on the molecule of chromophore (hem).
We should not exclude the fact that the formation of the process of photosensitization of the formation of oxyhemoglobin, and consequently the reaction of oxygen