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I'm not exactly sure, but it would seem to me that the mitochondria would add carbohydrates to proteins. The Golgi apparatus only packages and secretes waste.
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Why are most proteins destined for secretion from the cell glycoproteins?
because most proteins destined for secretion are glycoproteins (i.e. they are proteins with carbohydrates added to them); the carbohydrate is attached to the protein by enzymes.
What is the purpose of rough endoplasmic reticulum?
The rough endoplasmic reticulum is for making secretory proteins like enzymes and antibodies. The smooth endoplasmic reticulum produces steroids in certain cells and conducts impulse in muscle cells.
Is a polypeptide chain a carbohydrate?
No, peptide bonds are formed in proteins., this is incorrect they do form peptidoglycans which is a carbohydrate and amino acid mix.
What process takes place in the rough endoplasmic recticulum?
Ribosomes are found on an endoplasmic reticulum and those ribosomes create proteins that are inserted in the rough endoplasmic reticulum (ER) , where they may be chemically modified
Which cellular structure has single membrane?
Most of them. Lysosomes, endoplasmic reticulum, golgi apparatus, peroxisome, vacuoles all have single membranes. Nucleus has double membrane to make it less permeable, chloroplasts have membrane bound structures (thylakoid) inside its two membranes, and mitochondria have larger membrane that is folded within the outer membrane for added surface area.
The ER sends proteins and lipids it makes to what to be modified?
The endoplasmic reticulum (ER) sends proteins and lipids in membranous vesicles to the Golgi body (also known as the Golgi apparatus or the Golgi complex). The Golgi body looks like a stack of pita breads; it resembles the ER. There, the membranous vesicles containing proteins or lipids will fuse with one side of the Golgi body known as the cis face.Inside the Golgi body, proteins and lipids will have carbohydrate molecules added to them, forming glycoproteins (proteins with carbohydrates attached) and glycolipids (lipids with carbohydrates attached). After being modified, the glycoproteins and glycolipids will exit the Golgi body in membranous vesicles through the trans face (the side opposite the cisface).
Why do you called it Golgi complex?
From Wikipedia, the free encyclopediaThe Golgi complex, also known as the Golgi apparatus or simply the Golgi, is a cytoplasmic organelle. It is found in eukaryote cells, such as those of animals, plant, and fungi. It was discovered by Camillo Golgi in 1898. Golgi was ignored and his discovery was said to be dirt on his lenses. Years later, electron microscope pictures showed structures just like in the original Golgi drawings. It is made of several flattened sac-like membranes which some people say look like a stack of pancakes. The main function of the Golgi apparatus is to process and package macromolecules, such as proteins and lipids. They come to the Golgi after being built, and before they go to their destination. The Golgi complex inspects them for flaws and discards extra material added during their manufacture, wraps them up and then targets them for packaging. The Golgi complex is especially active in processing proteins for secretion. The Golgi releases special enzymes called lysosomes, which clean off any extra amino acids. When the package is ready, it is pinched off the Golgi and released into the cytoplasm. The Golgi complex is part of the cellular membrane system along with the endoplasmic reticulum. The Golgi apparatus is known as the powerhouse of the cell.
What is the relationship between the Golgi apparatus and plasma membrane?
Many proteins need additional sugars added to them. This is called glycosylation and is essential for many proteins and occurs in the Golgi, so if these proteins didn't pass through it there would be trouble. More importantly however is that many proteins need to be secreted, and they have to be secreted through the Golgi.
Where proteins are processed and packaged?
Proteins are produced in all cells by protein synthesis. It requires the mRNA molecule produced from DNA in nucleus. Once it is transported to cytoplasm, ribosomes and tRNA molecules and enzymes will carry out protein synthesis.
Why are most proteins destined for secretion from the cell glycoproteins?
because most proteins destined for secretion are glycoproteins (i.e. they are proteins with carbohydrates added to them); the carbohydrate is attached to the protein by enzymes.
What membrane surface molecules bind to proteins and serve as molecular identification tags?
molecular identification tags such as phosphate group added to the Golgi prouducts aid in sorting by acting like ZIP codes on mailing labels. BIOLOGY 8TH EDITHION ( CAMPBELL ET. AL 2008)
Does honey have Proteins?
About 0.5g or protein can be found in 100 g honey. Honey is a rich source of carbohydrates and not proteins. Honey can be added to the protein rich food that pair up well.
What is the purpose of rough endoplasmic reticulum?
The rough endoplasmic reticulum is for making secretory proteins like enzymes and antibodies. The smooth endoplasmic reticulum produces steroids in certain cells and conducts impulse in muscle cells.
Is a polypeptide chain a carbohydrate?
No, peptide bonds are formed in proteins., this is incorrect they do form peptidoglycans which is a carbohydrate and amino acid mix.
What is the Golgi job?
The Golgi apparatus, transports and organizes proteins. The Golgi traffics proteins made in the ER to the Golgi which then modifies them and sends them out to the cell wall. This is called the secretory pathway. The secretory pathway was mostly discovered by a man names Palade, he confirmed th existence of ribosomes. He used radioactive lysine which is called a pulse-chase experiment: Autoradiolgraphy provided evidence that proteins must go through the Golgi and that the mitochondria produced its own proteins. Once you radiolable the amino acid you can see where it goes through microscopy and you can also detect different modifications it goes through via an SDS page and a immunoprecipitate and another important technique is called the density gradient centrifuging. This type of differentiation though can only get the Golgi or microsomes (er). Lets talk about how the actual process occurs. N-linked glycosylation happens in the ER and is then tagged for transport to the Golgi apperatus. Firstly proteins cannot escape the secretory pathway then can go outside in the cytoplam. What is in the Golgi stays in the Golgi. So SAR 1 gets GTD to GDP from a transmembrane domain called SEC 12 then once it has GTP it can bind into the membrane and bind to SEC 23/24 which is involved in getting the actual cargo. Cargo binds to this SEC 23/24 and then binds SEC 13/31 which then pinches off the membrane. Once Sar 1 gets GTP to GDP the COPII coat dissociates to that all the little vesicals can form a VTC which is a pre-Golgi intermediate vessicle. So ER proteins lacking transmembranes domaisn connect interact directly with COPII SEC 23/24/ They must interact with ERGIC53 which is a corgo receptor that binds the N-linked oligosaccharides. Very few ER proteins are glysosylated. They return to the ER by retrograde because the cargo receptors can interact with CAP1. Basically COPI just recylces proteins to the ER. The vesicles move via moterproteisn like Dynesin to the Golgi from the ER. Nlinked oligosaccharides are needed to leave the VTC. VTC is almost a minature Golgi apperatus, the VTC is the pre-Golgi versicle. Once they arrive at the CIS-Golgi. The Golgi has 2 sections CIS and TRANS. They arrive in CIS and then travel to TRANS. Which there is contraversy about. The three main ideas are that of Intra Golgi trafficing are as follows. Simple Diffusion through the Cysternae of the Golgi. The cis cisternae could gradually mature to become the trans cisternae. (this was once a plausible because they saw the trans Golgi peeling off but now is unliked because they don't know how the enzymes stay in there approptiate cysternea) Then Rothman had dicovered the COP1 he proprosesed that the cargo just gets moved from one cysternae to another cia COP1 protein coat. Another experiement was done with stomatis virus G protein that linked the idea of maturation because all the contents stayed together. Either 2 ways are not looked at 1 Cop1 moves the enzymes back 2 The cysterane are linked together and they diffuse. Through either staying where they are needed or by the cholesterol pH gradient. pH is higher in the Trans. So once they are inside the Golgi cargo is processed. Sequential modification of the N-linked gylcosylation, the addition of an O-linked and and proteoglycan. So the N-acetylglucosamine GlcNac is the O-linked glycosilation that is added to the -OH on the serine. - happens in the middle. The removable mannose happens in CIS. along with sorting and phosphorlation The Galactose and the N-acetylneuraminic acid. - happen in the trans cisterna A good test to see if a cargo went through the Golgi is to use Endo-H. BEcause of the Nlink it will be resistance because of modification. All the proteolytic modifications required an acidic pH and remains acidic because of ATPase, raflomicin blacks this activity. Sorting. They are organized by kinasan molecules and are secreted to the baso or apical by membrane protein in the Trans Golgi. Budding from the Trans Golgi Cathrin is an important protein for the budding. Lipid rafts often found in the Trans Golgi that have proteins for export. Catherins are baskets used for endosomes and budding of the Golgi they are recruited by adapter proteins called AP1-3-4 and GGA. GGP soluble proteins AP3 proteins to the endosomes lysosomes, they help with the sorting as well as get clathrins. Once the catherins pinch of from the Golgi they Arf1 goes to GTP and de-coats and you get fusion of the wall and protein expulsion.
Where would you look on the food label to determine if sugar was added to product?
The carbohydrates. Carbohydrates are complex sugars.
Where would you look on the food label to determine if sugar was added to the product?
The carbohydrates. Carbohydrates are complex sugars.
