Glycosylation

... safe once again in a membrane bound organelle. Once inside the Golgi apparatus, the newly formed protein/enyzme will have its final modifications (glycosylation usually) that will then let the modified protein/enzyme bud off from the Golgi's membrane so that it is in its own membrane bound secretory ...

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... AMINO ACIDS as building blocks of protein (though there are close to 100 different amino acids that are observed in proteomics: phosphorylation, glycosylation, acetylation, and hydroxylations of the common amino acids are just a few of the modifications we know of so far).

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There are differences in glycosylation even among eukaryotes, and even among quite closely related species. Yeasts often over-glycosylate their products, although this is not to say they couldn't get it right in many cases. Even such ...

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as far as I know, glycosylation signals are conserved among all eukaryotes. For example, I just expressed chicken avidin into yeast and it gets glycosylated just fine

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A place you are likely to run into problems is in getting the pattern of glycosylation right. B cells & plasma cells attach sugars to antibodies. The pattern of glycosylation might be critical for interaction with other systems in the animal, such as T cells ...

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