Enzymatic Release of Sialic Acid

Enzymatic Release of Sialic Acid

Sialic acids are in exposed positions on macromolecules and cell surfaces and are potent modulators of cellular function. Therefore, their turnover or susceptibility to degrading enzymes is of interest for genetic diseases. CD BioGlyco has an efficient Enzymatic Release method to provide clients with sialic acid release service.

Sialic Acid

Glycosylation is a common post-translational modification that plays a crucial role in protein folding, trafficking, stability, and cellular activity. The two main types of glycosylation are N-glycosylation and O-glycosylation. Sialic acids are usually located on glycan terminal residues of N-glycosylation and O-glycosylation. They are a class of α-keto acid sugars composed of a nine-carbon skeleton and are one of the most important molecules in life. Sialic acids not only play an important role in the chemistry and biodiversity of glycoconjugates but is also closely related to many diseases, such as Salla disease, atherosclerosis, and influenza.

Fig.1 Common types of sialic acid-containing glycans on mammalian cells.Fig.1 Common types of sialic acid-containing glycans on mammalian cells. (Enterina, et al., 2019)

Sialidase is one of the most important enzymes in sialic acid catabolism. It removes sialic acid residues from the cell surface or serum sialic glycoconjugates. Typically, readily degradable glycoconjugates are captured by endocytosis in higher animals. Lysosomal sialidases remove sialic acid residues when late endosomes fuse with lysosomes. The activity of these sialidases is based on the removal of the O-acetyl group. A special form of sialidase is trans-sialidase, which combines the properties of sialidase and sialyltransferase. This enzyme prefers to transfer a sialic acid molecule from a glycoside to another sugar molecule, forming only an α-2,3 bond.

Since glycoprotein sialylation is critical to the bioavailability, stability, metabolism, and immunogenicity of protein therapeutics. Therefore, sialic acid is often released from glycoproteins in routine protein analysis. The content of sialic acid in the protein is then determined by various spectroscopic and chromatographic methods and its structure is characterized.

Sialic Acid Release Services

Sialic acid determination is performed by a variety of methods. Typically, sialic acid is released from glycoproteins by acid hydrolysis or enzymatic digestion before analysis. At CD BioGlyco, we have developed specialized Glycan Release platforms. To provide clients with efficient and accurate sialic acid release services from native glycoprotein or glycan structures. We completely release α2-3, α2-6, and α2-8-linked sialic acids present on N-glycans and O-glycans under the action of sialidases. In addition, we also provide fast and sensitive Sialic Acid Analysis services through high-performance anion-exchange chromatography with pulsed amperometric detection (HPAEC-PAD), liquid chromatography-mass spectrometry (LC-MS), etc.

Fig.2 The process of enzymatic release of sialic acid. Fig.2 The process of enzymatic release of sialic acid. (CD BioGlyco)

Applications

  • Glycosylation modification research
  • Identification of glycan structures on glycoproteins
  • Eliminate sialic acid residues at the ends of glycans
  • Analysis of abnormal sialylation

Advantages of Us

  • Release of sialic acid on N-glycans and O-glycans
  • Release α2-3, α2-6, and α2-8-linked sialic acids
  • Fast and accurate release of sialic acid
  • Professional sialic acid analysis service

CD BioGlyco has quite a wealth of experimental experience in the enzymatic release of sialic acid. Our advanced experimental equipment and experienced researchers provide a guarantee for clients' experimental results. If you are interested in our enzymatic release of sialic acid, please contact us for more detailed information.

References:

  1. van Karnebeek, C.D.; et al. NANS-mediated synthesis of sialic acid is required for brain and skeletal development. Nature Genetics. 2016, 48(7): 777-784.
  2. Enterina, J.R.; et al. Coordinated roles for glycans in regulating the inhibitory function of CD22 on B cells. Biomedical journal. 2019, 42(4): 218-232.
This service is for Research Use Only, not intended for any clinical use.

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