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What concentration of glucose causes glycosylation?
Hemoglobin is glycosylated at any concentration, even normal blood sugar levels. This is why there is a "normal" hemoglobin A1c range. The problem comes when there is an elevated blood glucose. The problem is with the elevated blood glucose, not that there is an elevated Hgb A1c. The A1c is only a marker and a way for physicians to measure the average blood glucose over the past 120 days.
What completes final modifications of protein?
The process of protein modifications is typically completed in the Golgi apparatus of the cell. During this process, the proteins undergo various post-translational modifications, such as glycosylation, phosphorylation, and cleavage. These modifications are essential for the proper functioning and localization of the proteins within the cell.
Which mechanisms of controlling gene expression occurs outside of the nucleus?
Translation, which is the process of protein synthesis, occurs outside of the nucleus in the cytoplasm. Post-translational modifications of proteins, such as phosphorylation and glycosylation, also occur outside of the nucleus. These modifications can alter the function, stability, and localization of proteins.
Post translational modification occurs in which cell organelle?
Post-translational modifications occur in the endoplasmic reticulum and Golgi apparatus, as well as in other cellular compartments. These modifications can include phosphorylation, glycosylation, acetylation, and more, which help to regulate protein function and localization within the cell.
What are the genetic disorders associated with oligosaccharides?
Defective Enzyme Disorder: includes the following: α-Mannosidosis α-Mannosidase β-Mannosidosis β-Mannosidase α-Fucosidosis α-Fucosidase Sialidosis α-Neuraminidase Galactosialidosis Protective protein Aspartylglucosaminuria Aspartylglycosaminidase Schindler disease α-N-Ac-galactosaminidase Mucolipidosis II (I-cell disease) N-acetylglycosmaine-1 phosphotransferase Mucolipidosis III N-acetylglycosmaine-1- phosphotransferase.
Why does glycosylation of hemoglobin take place?
glycosylation
Where does glycosylation of proteins occur?
Glycosylation of proteins occurs in the endoplasmic reticulum (ER) and Golgi apparatus within the eukaryotic cells. In the ER, initial glycosylation processes take place, and then the proteins are further modified in the Golgi apparatus before being transported to their final destinations inside or outside the cell.
What are the roles of N-linked and O-linked glycosylation in protein structure and function?
N-linked glycosylation helps with protein folding, stability, and recognition of the protein by other molecules. O-linked glycosylation can affect protein function by regulating protein activity, localization, and interactions with other molecules. Both types of glycosylation play important roles in modifying protein structure and function.
Mention the functions of Golgi body in plants?
protein glycosylation, lipid glycosylation and also Golgi works as a secretory point; from Golgi, secretory vesicles bud.
What is the Portuguese translation for alterations in glycosylation?
It's "Alterações na Glicosilação"
What are three types of post-translational modification?
methylation lipidation glycosylation phosphorylation
Where does glycosylation of proteins occur in mammalian cell?
In both the Endoplasmic Reticulum and the Golgi complex.
What is N glycosylation and where does it occur?
N-glycosylation is a post-translational modification process where carbohydrate moieties are attached to the nitrogen atom of asparagine residues in proteins. This modification typically occurs in the endoplasmic reticulum (ER) and continues in the Golgi apparatus, playing a crucial role in protein folding, stability, and cellular signaling. N-glycosylation is essential for the proper function of many glycoproteins, which are involved in various biological processes.
How can glycosylation affect protein solubility?
Glycosylation can significantly influence protein solubility by altering the protein's surface properties and overall conformation. The addition of carbohydrate moieties can enhance hydrophilicity, promoting interactions with water and preventing aggregation, which often improves solubility. Conversely, improper or excessive glycosylation may lead to misfolding or increased hydrophobic regions, potentially decreasing solubility. Thus, the specific structure and composition of glycan chains play a crucial role in determining protein solubility.
Is thyrogine a amino acid?
i think you mean..thyrogen? Thyrogen is comprised of two non-covalently linked subunits, an alpha subunit of 92 amino acid residues containing two N-linked glycosylation sites and a beta subunit of 118 residues containing one N-linked glycosylation site. The amino acid sequence of thyrotropin alfa is identical to that of human pituitary thyroid stimulating hormone.
What concentration of glucose causes glycosylation?
Hemoglobin is glycosylated at any concentration, even normal blood sugar levels. This is why there is a "normal" hemoglobin A1c range. The problem comes when there is an elevated blood glucose. The problem is with the elevated blood glucose, not that there is an elevated Hgb A1c. The A1c is only a marker and a way for physicians to measure the average blood glucose over the past 120 days.
What is the molecular weight for invertase?
For yeast invertase, the cytoplasmic form is 135kDa. The excreted form is 270kDa due to heavy glycosylation
