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Changes in human γ-globulin preparations during storage

Изменения в правах γ-Глобулин препарато в во время хранения

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Summary

During storage, human γ-globulin preparations undergo slow proteolysis, resulting in the formation of two split fractions. One of these (γx) is slower than normal γ-globulin, while the other (γy) is more rapid. The rate of breakdown in plasma preparations covers several years, while in preparations derived from haemolysed and placental material it is several months. Similar breakdown was induced by plasmin, trypsin and papain. The change can best be detected by immunoelectrophoresis, but electrophoresis in agar and high-speed centrifugation also give an approximate picture of the state of the preparation.

The γx fraction can be recovered in an immunoelectrophoretically pure state by precipitation with ammonium sulphate (over 50% saturation) or with Zn2+ salts (in the supernatant fluid at over 50 mM concentration). The γy fraction crystallizes out of solutions with low ionic strength in the form of minute, needle-like, optically inactive crystals.

The causes of the changes in the respective preparations and the biochemical and immunochemical aspects of the given phenomenon are discussed.

Abstract

Во время хранения, человека γ-глобулин препараты протеолиза проходить медленно, в результате в составе двух фракций сплит. Один из них (γx) медленнее, чем обычно γ-глобулин, в то время как другие (γи) больше быстрыми темпами. Темпы разрушения в плазме подготовка охватывает несколько лет, тогда как в препаратов, полученных в результате haemolysed и плацентарной материала это несколько месяцев. Аналогичная разбивка была искусственно вызванной в плазмин, trypsin и papain. Определенный артикль изменения могут быть обнаружены путем immunoelectrophoresis, но электрофореза в Агар и высокоскоростного центрифугирования также дают приблизительную картину состояния подготовки.

Определенный артикль γx дроби могут быть восстановлены в immunoelectrophoretically чистом состоянии путем осадков с сульфата аммония (более 50% насыщения), или с Zn2+ солей (в supernatant жидкости составляет более 50 мм концентрация). Определенный артикль γи фракция crystallizes из решений с низкой ионной силы в виде минуту, игла-как, оптически неактивных кристаллов.

Причины изменений в соответствующую препаратов и биохимических и Иммунохимические аспекты с учетом явления рассматриваются.

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Authors and Affiliations

  1. Institute of Sera and Vaccines, Prague

    F. Škvařil

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  1. F. Škvařil
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Additional information

During the time this paper was in press a study by H. E. Schultze was published concerning the gamma X globulin and its relation to reactive protein (Klin. Wschr. 37: 62, 1960). Yet in this case the author does not describe the fraction mentioned in our paper; it is a case a unintentional congruity in nomenclature.

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Škvařil, F. Changes in human γ-globulin preparations during storage. Folia Microbiol 5, 264–271 (1960). https://doi.org/10.1007/BF02928159

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