Download e-book for kindle: Биологические мотивации by Судаков К.В.

By Судаков К.В.

ISBN-10: 1597454443

ISBN-13: 9781597454445

ISBN-10: 1934115118

ISBN-13: 9781934115114

;Биологические мотивации КНИГИ ;НАУКА и УЧЕБА Автор: Судаков К.В. Название: Биологические мотивации Издательство: Медицина Год: 1971 Формат: djvu Размер: 4,6 Mb +3% Для сайта: www.mirknig.comКнига посвящена описанию таких эмоциональных состояний как голод, жажда, половое возбуждение, страх. Показана роль мотивации в приспособительных реакциях организма, патология и психофармакология мотиваций.Depozit documents zero

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This suspension is then centrifuged at 17,000g in a Sorval GSA rotor for 30 min at 4°C, which pellets the cell membranes and other debris. The clarified cell extract, the supernatant, contains the soluble protein from the cell and is applied directly to the Fast Q column. 3. Fast Q chromatography 1. The extract is applied at a flow rate of 6 mL/min to the Fast Q anion-exchange column, which was pre-equilibrated with buffer A. 2. The column was then washed with 500 mL buffer A (5 mL/min) and proteins are eluted with a linear gradient of 50 mM to 1 M NaCl (100% buffer A to 100% buffer B).

The following staining method can be used for all gel electrophoreses described in the protocol. 1. 1% Commassie brilliant blue R250, 60% H20 (v/v). 2. Destain I: 10% (v/v) acetic acid, 30% (v/v) methanol, 60% H20 (v/v). 3. Destain II: 10% acetic acid, 10% glycerol, 80% H20 (v/v) (see Note 2). 7. Protein Concentration Two methods are employed for the concentration of crude extract or protein solutions during the purification protocol. 1. Nitrogen-pressurized stirred cell (Amicon): For concentration of large volumes, 50–1000 mL, we use the stirred cell according to the manufacturer’s instructions at a pressure of 50 psi.

2. The column is pre-equilibrated with buffer C, which contains 20% ethanol. In comparative runs, including and omitting alcohols, it was found that buffer C produced the purest GroEL. It is thought that the ethanol is effective in releasing GroEL-bound proteins/peptides, leading to a much cleaner preparation. At present, the underlying reason for this is not clearly understood. 3. 5 mL/min, and fractions of 5 mL are collected. Chaperonin elutes in a sharp peak close to void volume. Those fractions containing GroEL are identified by 4–15% native PAGE (8 µL sample, 2 µL loading buffer, and 1 µL applied to gel) and pooled.

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Биологические мотивации by Судаков К.В.


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