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Европейская фармакопея 6.01 >>>
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| Автор | Тема: Европейская фармакопея 6.01 | ||
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N-Виталий Пользователь Ранг: 630 |
 06.07.2007 // 6:38:53
Редактировано 2 раз(а) Здравствуйте коллеги. Решил последовать примеру и поиграть в доброго самаритянина. Имеется Европейская Фармакопея 5.0 последние издание полное собрание, на бумаге. Кому очень надо обращайтесь, только желательно указывать точный адресс (том страница или ссылка на статью), а ещё лучше номер страницы (там непрерывная нумерация с первого по десятый тома). Сразу оговорюсь большие объёмы выслать не смогу (сканер плохой). 
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ANCHEM.RU Администрация Ранг: 246 |
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varban VIP Member Ранг: 8699 |
06.07.2007 // 9:23:50
У нас дома есть электронная 2000, которая 3 издание. Кроме того, есть и британская 2000. Более новые электронные попадались, но времени разобраться с защитой не было
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N-Виталий Пользователь Ранг: 630 |
06.07.2007 // 9:28:23
Мы специально не стали брать електронный вариант, неизвестно, как он пойдет на наших машинах, "винда" фирменная не везде есть, а бумаге, что станется?! к тому же не дай бог електронная версия полетит? начальство три шкуры спустит, оно и так чуть не удавилось когда нам эту покупало
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Griseus Пользователь Ранг: 2 |
09.08.2007 // 7:53:41
Требуется вся информация по контроль качества Апротинина. Если можно в кройчайшие сроки. P.S: или скажите откуда можно скацать ее в электроном виде? |
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DSP007 VIP Member Ранг: 2228 |
09.08.2007 // 10:48:43
Нифига себе вопрос, у него разные лекарственные формы... А кроме фармакопейных методик есть еще и различные научные работы по его анализу... Хоть бы уточнили, чего треба Но ладно, сегодня я добрый, цитата из BP2000 1/00 Aprotinin complies with the requirements of the 3rd edition of the European Pharmacopoeia [0580]. These requirements are reproduced after the heading 'Definition' below. Action and use Proteolytic enzyme inhibitor. Preparation Aprotinin Injection Ph Eur DEFINITION Aprotinin is a polypeptide consisting of a chain of fifty-eight amino acids. It inhibits stoichiometrically the activity of several proteolytic enzymes such as chymotrypsin, kallikrein, plasmin and trypsin. It contains not less than 3.0 European Pharmacopoeia Units of aprotinin activity per milligram, calculated with reference to the dried substance. PRODUCTION Where applicable, it complies with the monograph on <nop select BODY scroll +fi WIXLINK1052>Products with risk of transmitting agents of animal spongiform encephalopathies (1483). The animals from which aprotinin is derived must fulfil the requirements for the health of animals suitable for human consumption to the satisfaction of the competent authority. It must have been shown to what extent the method of production allows inactivation or removal of any contamination by viruses or other infectious agents. The method of manufacture is validated to demonstrate that the product, if tested, would comply with the following tests: Abnormal toxicity (2.6.9). Inject into each mouse a quantity of the substance to be examined containing 2 Ph. Eur. U. dissolved in a sufficient quantity of water for injections R to give a volume of 0.5 ml. Histamine (2.6.10). Not more than 0.2 µg of histamine base per 3 Ph. Eur. U. CHARACTERS An almost white powder, hygroscopic, soluble in water and in isotonic solutions, practically insoluble in organic solvents. IDENTIFICATION A. Examine by thin-layer chromatography (2.2.27), using a TLC silica gel G plate R. Test solution. Use solution S (see Tests). Reference solution. Use aprotinin solution BRP. Apply separately to the plate to 10 µl of each solution. Develop over a path of 12 cm using a mixture of 80 volumes of water R and 100 volumes of glacial acetic acid R containing per millilitre of mixture 0.10 g of sodium acetate R. Allow the plate to dry in air and spray with a solution of 0.1 g of ninhydrin R in a mixture of 6 ml of a 10 g/l solution of cupric chloride R, 21 ml of glacial acetic acid R and 70 ml of ethanol R. Dry the plate at 60°C. The principal spot in the chromatogram obtained with the test solution is similar in position, colour and size to the principal spot in the chromatogram obtained with the reference solution. B. Determine the ability of the substance to be examined to inhibit trypsin activity using the method described below. Test solution. Dilute 1 ml of solution S to 50 ml with buffer solution pH 7.2 R. Trypsin solution. Dissolve 10 mg of trypsin CRS in 0.002M hydrochloric acid and dilute to 100 ml with the same acid. Casein solution. Dissolve 0.2 g of casein R in buffer solution pH 7.2 R and dilute to 100 ml with the same buffer solution. Precipitating solution. Mix 1 volume of glacial acetic acid R, 49 volumes of water R and 50 volumes of ethanol R. Mix 1 ml of the test solution with 1 ml of the trypsin solution. Allow to stand for 10 min and add 1 ml of the casein solution. Incubate at 35°C for 30 min. Cool in iced water and add 0.5 ml of the precipitating solution. Shake and allow to stand at room temperature for 15 min. The solution is cloudy. Carry out a blank test under the same conditions using buffer solution pH 7.2 R instead of the test solution. The solution is not cloudy. TESTS Solution S Prepare a solution of the substance to be examined containing 15 Ph. Eur. U. per millilitre, calculated from the activity stated on the label. Appearance of solution Solution S is clear (2.2.1). Absorbance (2.2.25). Prepare a solution of the substance to be examined containing 3.0 Ph. Eur. U. per millilitre. The solution shows an absorption maximum at 277 nm. The absorbance at the maximum is not greater than 0.80. Protein impurities of higher molecular mass Examine by size-exclusion chromatography (2.2.30), using cross-linked dextran for chromatography R2. Use a 180 g/l solution of anhydrous acetic acid R to swell the gel and as the eluent. Prepare a column of gel 0.8 m to 1.0 m long and 25 mm in diameter, taking care to avoid the introduction of air bubbles. Place at the top of the column a quantity of the substance to be examined containing 300 Ph. Eur. U. dissolved in 1 ml of a 180 g/l solution of anhydrous acetic acid R and allow to elute. Collect the eluate in fractions of 2 ml. Measure the absorbance (2.2.25) of each fraction at the absorption maximum at 277 nm and plot the values on a graph. The chromatogram obtained does not present an absorption maximum before the elution of the aprotinin. Loss on drying (2.2.32). Not more than 6.0 per cent, determined on 0.100 g by drying in vacuo. Sterility (2.6.1). If intended for use in the manufacture of parenteral dosage forms without a further appropriate sterilisation procedure, it complies with the test for sterility. Pyrogens (2.6.8). If intended for use in the manufacture of parenteral dosage forms without a further appropriate procedure for the removal of pyrogens, it complies with the test for pyrogens. Inject per kilogram of the rabbit's mass 1 ml of a solution of the substance to be examined containing 15 Ph. Eur. U. per millilitre. ASSAY The activity of aprotinin is determined by measuring its inhibitory action on a solution of trypsin of known activity. The inhibiting activity of the aprotinin is calculated from the difference between the initial activity and the residual activity of the trypsin. The inhibiting activity of aprotinin is expressed in Ph. Eur. Units. 1 Ph. Eur. U. inhibits 50 per cent of the enzymatic activity of 2 microkatals of trypsin. Use a reaction vessel with a capacity of about 30 ml and provided with: a device that will maintain a temperature of 25±0.1°C; a stirring device, such as a magnetic stirrer; a lid with five holes for accommodating the electrodes, the tip of a burette, a tube for the admission of nitrogen and the introduction of the reagents. An automatic or manual titration apparatus may be used. In the latter case the burette is graduated in 0.05 ml and the pH meter is provided with a wide reading scale and glass and calomel electrodes. Test solution. Prepare a solution of the substance to be examined in 0.0015M borate buffer solution pH 8.0 R expected to contain 1.67 Ph. Eur. U. per millilitre (about 0.6 mg (m mg) per millilitre). Trypsin solution. Prepare a solution of trypsin CRS containing about 0.8 microkatals per millilitre (about 1 mg per millilitre), using 0.001M hydrochloric acid as the solvent. Use a freshly prepared solution and keep in iced water. Trypsin and aprotinin solution. To 4.0 ml of the trypsin solution add 1.0 ml of the test solution. Dilute immediately to 40.0 ml with 0.0015M borate buffer solution pH 8.0 R. Allow to stand at room temperature for 10 min and then keep in iced water. Use within 6 h of preparation. Dilute trypsin solution. Dilute 0.5 ml of the trypsin solution to 10.0 ml with 0.0015M borate buffer solution pH 8.0 R. Allow to stand at room temperature for 10 min and then keep in iced water. Maintain an atmosphere of nitrogen in the reaction flask and stir continuously; introduce 9.0 ml of 0.0015M borate buffer solution pH 8.0 R and 1.0 ml of a freshly prepared 6.9 g/l solution of benzoylarginine ethyl ester hydrochloride R. Adjust to pH 8.0 by the addition of 0.1M sodium hydroxide. When the temperature has reached equilibrium at 25±0.1°C, add 1.0 ml of the trypsin and aprotinin solution and start a timer. Maintain at pH 8.0 by the addition of 0.1M sodium hydroxide and note the volume added every 30 s. Continue the reaction for 6 min. Determine the number of millilitres of 0.1M sodium hydroxide used per second (n1 ml). Carry out, under the same conditions, a titration using 1.0 ml of the dilute trypsin solution. Determine the number of millilitres of 0.1M sodium hydroxide used per second (n2 ml). Calculate the aprotinin activity in Ph. Eur. units per milligram from the expression: [bitmap] The estimated activity is not less than 90 per cent and not more than 110 per cent of the activity stated on the label. STORAGE Store in an airtight, tamper-proof container, protected from light. LABELLING The label states: — the number of Ph. Eur. Units of aprotinin activity per milligram, — where applicable, that the substance is sterile, — where applicable, that the substance is apyrogenic. Ph Eur |
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Griseus Пользователь Ранг: 2 |
09.08.2007 // 11:09:19
Там помойме страницы 1015-1016 что так |
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Каталог ANCHEM.RU Администрация Ранг: 246 |
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Babykat Пользователь Ранг: 1 |
15.08.2007 // 19:20:15
Редактировано 1 раз(а)
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N-Виталий Пользователь Ранг: 630 |
16.08.2007 // 7:59:06
скинул, принимайте. |
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Багира Пользователь Ранг: 2 |
26.10.2007 // 19:34:03
Редактировано 1 раз(а) Пользователь удалил свое сообщение |
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Багира Пользователь Ранг: 2 |
26.10.2007 // 19:34:58
Помогите пожалуйста. Очень нужны страницы с содержанием из Европейской Фармакопии или из американской фармакопеи на тему ВЭЖХ Липоевой кислоты. Заранее спасибо. znataliag{coбaчkа}rambler.ru |
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N-Виталий Пользователь Ранг: 630 |
29.10.2007 // 7:20:33
Не понял!? содержание, или статья на Липоевую кислоту?? |
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Ответов в этой теме: 67
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