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Clindamycin

By H. Jared. Wentworth Institute of Technology. 2017.

Other tissues order 150mg clindamycin visa, such as the liver cheap 150mg clindamycin with mastercard, brain, and red blood cells, have a different type of glucose transporter that is not as significantly affected by Glucose insulin. Metabolic differences exist between these tissues (see + Chapter 28), but, in essence, insulin stimulates glycogen synthesis in resting mus- Glycogen cle as it does in the liver. A key difference between muscle and liver is that insulin greatly stimulates the transport of glucose into muscle cells but only slightly stim- Muscle ulates its transport into liver cells. RETURN OF BLOOD GLUCOSE TO FASTING LEVELS C Glucose VLDL After a meal has been digested and absorbed, blood glucose levels reach a peak and then begin to decline. The uptake of dietary glucose by cells, particularly those in + + the liver, muscle, and adipose tissue, lowers blood glucose levels. By 2 hours after FA a meal, blood glucose levels return to the normal fasting level of less than 140 mg/dL. Blood Glucose Levels in the Fasting State Pyruvate 1. CHANGES IN INSULIN AND GLUCAGON LEVELS + FA During fasting, as blood glucose levels decrease, insulin levels decrease, and CO + H O Triacylglycerol 2 2 glucagon levels rise. These hormonal changes cause the liver to degrade glycogen by the process of glycogenolysis and to produce glucose by the process of gluco- Adipose cell neogenesis so that blood glucose levels are maintained. Glucose metabolism in various tis- Within a few hours after a high-carbohydrate meal, glucagon levels begin to rise. Effect of insulin on glycogen synthesis Glucagon binds to cell surface receptors and activates adenylate cyclase, causing and degradation and on VLDL synthesis in the liver. Glucose metabolism in resting muscle cAMP levels in liver cells to rise (Fig. The transport of glucose into which phosphorylates and inactivates glycogen synthase. Therefore, glycogen cells and the synthesis of glycogen are stimu- synthesis decreases. Glucose metabolism in adi- At the same time, protein kinase A stimulates glycogen degradation by a two- pose tissue in the fed state. Protein kinase A phosphorylates and activates phosphorylase DHAP dihydroxyacetone phosphate.

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N-linked oligosaccharides are found attached to cell surface proteins discount clindamycin 150 mg free shipping, where they protect the cell from proteolysis or an immune attack generic 150mg clindamycin with mastercard. In contrast, an O-glycosidic link is a common way of attaching oligosac- charides to the serine or threonine hydroxyl groups in secreted proteins. The intra- cellular polysaccharide glycogen is attached to a protein through an O-glycosidic linkage to a tyrosine. Fatty Acylation or Prenylation Many membrane proteins contain a covalently attached lipid group that interacts hydrophobically with lipids in the membrane. Palmitoyl groups (C16) are often attached to plasma membrane proteins, and the myristoyl group (C14) is often Adenylyl cyclase is posttranslation- attached to proteins in the lipid membranes of intracellular vesicles (see Fig. The farnesyl (C15) or geranylgeranyl group (C20) are synthesized from an oligosaccharide chain attached the five-carbon isoprene unit (isopentenyl pyrophosphate, see Fig. These are attached in ether linkage to a specific of the isozymes contain serine residues on cysteine residue of certain membrane proteins, particularly proteins involved in the intracellular portion of the chain that regulation. Regulatory Modifications Phosphorylation, acetylation, and adenosine diphosphate (ADP)-ribosylation of specific amino acid residues in a polypeptide can alter bonding by that residue and change the activity of the protein (see Fig. Phosphorylation of an OH group on serine, threonine, or tyrosine by a protein kinase (an enzyme that trans- fers a phosphate group from ATP to a protein) introduces a large, bulky, nega- tively charged group that can alter the activity of a protein. Reversible acetylation occurring on lysine residues of histone proteins in the chromosome changes their 86 SECTION TWO / CHEMICAL AND BIOLOGICAL FOUNDATIONS OF BIOCHEMISTRY Carbohydrate addition O-glycosylation: OH of ser, thr, tyr, N-glycosylation: NH2 of asn O H O CH2 CH2 R O R O ser asn N N AC AC Lipid addition Palmitoylation: Internal SH of cys Myristoylation: NH of N-terminal gly O O O H3C (CH2)14 C S CH2 H3C (CH2)12 C N CH2 C H cys gly Prenylation: SH of cys O Cys C OCH3 SH O CH3 CH3 Cys C OCH3 CH3 C (CH2 CH2)2 H Regulation Phosphorylation: OH of ser, thr, tyr Acetylation: NH2 of lys, terminus O O CH O P O– CH C N CH CH CH CH 2 3 2 2 2 2 H O– ser arg ADP-ribosylation: N of arg, gln; S of cys + O O NH2 H Adenine CH2 P CH2 N C CH2 CH2 CH2 O – – O O O arg H HO OH HO OH Modified amino acids Oxidation: pro, lys Carboxylation: glu O N CH C CH2 pro H2 2 glu C CH –COO COO– H 4-Hydroxyproline γ–Carboxyglutamate residue Fig. Posttranslational modifications of amino acids in proteins. Some of the com- mon amino acid modifications and the sites of attachment are illustrated. Because these modifications are enzyme-catalyzed, only a specific amino acid in the primary sequence is altered. In N-glycosylation, the attached sugar is usually N-acetylglucosamine (N-Ac). CHAPTER 6 / AMINO ACIDS IN PROTEINS 87 interaction with the negatively charged phosphate groups of DNA.

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