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1.
Technol Cancer Res Treat ; 10(6): 507-17, 2011 Dec.
Article in English | MEDLINE | ID: mdl-22066592

ABSTRACT

A portable rectal near infrared (NIR) scanning polarization imaging unit with an optical fiber-based rectal probe, designated as a Photonic Finger (PF), was designed, developed, built and tested. PF was used to image and locate the three dimensional (3D) positions of abnormal prostate tissue embedded inside normal prostate tissue. An inverse image reconstruction algorithm, namely Optical Tomography using Independent Component Analysis (OPTICA) was developed to unmix the signal from targets (cancerous tissue) embedded in a turbid media (normal tissue) in the backscattering imaging geometry. The Photonic Finger combined with OPTICA was ex vivo tested to characterize different target(s) inside different tissue medium, including cancerous prostate tissue embedded inside large pieces of normal tissue. This new developed instrument, Photonic Finger, may provide an alternative imaging technique, which is accurate, of high spatial resolution and non-or-less invasive for prostate cancers screening.


Subject(s)
Early Detection of Cancer , Infrared Rays , Photons , Prostate/pathology , Prostatic Neoplasms/diagnosis , Tomography, Optical/instrumentation , Tomography, Optical/methods , Algorithms , Animals , Chickens , Computer Simulation , Female , Humans , Male , Mammary Glands, Animal/pathology
2.
Mol Biol (Mosk) ; 39(2): 330-5, 2005.
Article in Russian | MEDLINE | ID: mdl-15856957

ABSTRACT

Equilibrium unfolding of apomyoglobin by urea was investigated in the temperature range from 5 to 25 degrees C at two pH values. The thermodynamic parameters of the apomyoglobin native-unfolded state transition were determined. Conformational changes in the protein structure were monitored by tryptophan fluorescence and far UV circular dichroism. Apomyoglobin preserves its native conformation at pH 5.7 and 6.2 in the temperature range used. It was shown that the apomyoglobin stability and its unfolding cooperativity are substantially lower at 5 degrees C than at other temperatures. This fact should be taken in account at the investigation of apomyoglobin.


Subject(s)
Apoproteins/chemistry , Hydrogen-Ion Concentration , Myoglobin/chemistry , Temperature , Urea/chemistry , Circular Dichroism , Thermodynamics
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