ENZYME ENTRAPMENT IN LIPOSOMES

ENZYME ENTRAPMENT IN LIPOSOMES
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DOI:
10.1016/0014-5793(71)80109-6
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发表时间:
1971-01-01
期刊:
影响因子:
3.5
通讯作者:
RYMAN, BE
RYMAN, BE
中科院分区:
生物学3区
文献类型:
--
作者:
GREGORIA.G;LEATHWOO.PD;RYMAN, BE

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Enzyme replacement therapy for patients with various disorders in which a specific enzyme activity is absent from one or more tissues, has been attempted in several instances by direct administration to the patient of an enzyme designed to remove undesirable accumulation products [IS]. However, apart from the possible immunological response that could arise from the foreign protein, there are also the problems related to undesirability of having certain enzymes in the circulation and of directing the given protein to a particular tissue.We thought that some of the difficulties mentioned could be circumvented by entrapping proteins into liposomes (lipid spherules). Liposomes are formed when phospholipids are allowed to swell in aqueous media and become hydrated liquid crystals. These, when suitably dispersed, consist of a series of concentric bilayers which alternate with aqueous compartments in which can be entrapped water-soluble substances [6, 7]. The present paper describes the entrapment ofAsper-giZlus niger amyloglucosidase (EC 3.2. 1.3.) and albumin into liposomes. The choice of the amyloglucosidase in this entrapment investigation reflects our interest in the glycogen storage diseases, while the commercial availability of r3r I-albumin has provided a readily detectable protein, similar in both molecular size and charge to the amyloglucosidase.