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1.
J Photochem Photobiol B ; 189: 49-54, 2018 Dec.
Article in English | MEDLINE | ID: mdl-30312920

ABSTRACT

STUDY DESIGN: Application of Photobiomodulation therapy (PBMT) and meloxicam in acute spinal cord injury, functional recovery and histological evaluation. OBJECTIVE: Evaluation of the effect of simultaneous PBMT and meloxicam on treatment of acute experimental spinal cord injury and comparing it with the effect of application of each of them separately. SETTING: The study was conducted at the Department of Surgery & Radiology, Faculty of Veterinary Medicine and Institute of Biomedical Research, University of Tehran, Tehran, Iran. METHODS: Twenty four rats were used in this study. A compression injury was induced to the T8-T9 segment of the spinal cord of rats using a Fogarty embolectomy catheter. Rats were randomly divided into 4 groups including: Control group, PBMT (810 nm-200 mw-8 s-2 weeks) group, Meloxicam (1 mg/kg) group, and PBMT and Meloxicam (mixed) group. After inducing injury, hind limb performance of the rats was evaluated, using BBB test and then treatment intervention was performed and continued for 2 weeks. RESULTS: Four  weeks after injury induction, BBB test results were significantly higher in all treatment groups in comparison to control group, however, there were no significant differences among the treatment groups. In addition, histological findings revealed no significant difference between all 4 study groups. CONCLUSION: According to the results of this study we can conclude that simultaneous and separate application of PBMT and Meloxicam play an effective role in treatment of acute spinal cord injuries.


Subject(s)
Low-Level Light Therapy/methods , Meloxicam/therapeutic use , Spinal Cord Injuries/therapy , Animals , Anti-Inflammatory Agents, Non-Steroidal/therapeutic use , Combined Modality Therapy/methods , Rats , Treatment Outcome
2.
Indian J Biochem Biophys ; 42(5): 326-9, 2005 Oct.
Article in English | MEDLINE | ID: mdl-23923542

ABSTRACT

The interaction of alpha-amylase (from Bacillus amyloliquefaciens) with Mg2+ ion was studied using UV spectrophotometric and isothermal titration calorimetric (ITC) methods at 27 degrees C in 30 mM Tris buffer solution at pH = 7.0. The binding isotherm for metal-protein interaction was easily obtained by carrying out ITC experiment at two different concentrations (2 microM and 50 microM) of the protein. Alpha-Amylase had eight identical and independent binding sites for Mg2+ ion, which showed non-cooperativity in the binding process. The binding of Mg2+ ion was exothermic (deltaH= -17.3 kJ mol(-1)) with association binding constant of 2.08 mM(-1). The binding slightly destabilized the enzyme against thermal denaturation, as evident from absorption studies.


Subject(s)
Bacillus/enzymology , Magnesium/metabolism , Thermodynamics , alpha-Amylases/metabolism , Binding Sites , Calorimetry , Enzyme Stability , Magnesium/chemistry , Protein Binding , Protein Denaturation , Spectrophotometry, Ultraviolet , alpha-Amylases/chemistry
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