Titlebook: Glyco-and Cellbiology; Biosynthesis, Transp Felix Wieland,Werner Reutter Conference proceedings 1994 Springer-Verlag Berlin Heidelberg 1994

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https://doi.org/10.1007/978-3-319-27359-4n vitro, did not require the presence of antigen to obtain their specific binding property (Haber 1964; Whitney and Tanford 1965). From Anson’s observations that denatured hemoglobin could be converted back into native protein (Anson 1945), it became obvious that the amino acid sequence contained al

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Lee‘s Ophthalmic Histopathologye general outline of the secretory pathway. The basics of this pathway are now well established. Nascent proteins are targeted to the first organelle of this pathway, the endoplasmic reticulum, via a signal sequence (Blobel and Dobberstein 1975). Subsequently, proteins are transported in a vectorial

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,A mesoparasitic barnacle – Anelasma, Golgi network (TGN) (Griffiths and Simons 1986). Up until this point, transport occurs by default, no signals being needed for proteins to move from the ER to the Golgi and from cis-terna to cisterna within the stack (Rothman and Orci 1992). This immediately raises the question of how proteins are

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Doorverwijzing en vergoede interventiesat degrade a wide spectrum of macromolecules including proteins, lipids, nucleic acids, and polysaccharides into their monomeric constituents. The bulk of these acid hydrolases and of their cofactors are soluble components of the lysosomal matrix. The lysosomal membrane separates the potentially hos

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Marike Lancel,Inge Ensing,Maaike van Veens obvious that the behavior of a membrane protein is dependent upon its lipid environment. The interplay between proteins and lipids during membrane trafficking is, however, an area of research that has been largely neglected. Interest in the glycolipid-dependent sorting of proteins in membranes is

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