How does a 40% decrease in albumin affect the total protein content when the albumin loss is rapid?
361509
did u mean total albumin content of the blood? coz proteins make up mostly everything - enzymes, celss, etc. albumin is mainly a non-specific transport protein which serves a very important role in being non-selective. in the blood it consists most of total protein and rapid loss of albumin decreases the blood's colloid osmotic pressure as total protein decreases. this will lead to edema and increased urine output.
822272
Water, of course, is liberated. If hydrolysis is complete, the protein is broken down into free amino acids. If hydrolysis is only partial, then the protein is broken up into fragments. If partial hydrolysis is performed on the folded protein then the lesions often occur at solvent-exposed loops, and particular fragments are the result.
333768
Losing weight that quickly can be dangerous.\nRapid weight loss and restrictive diets can deplete muscle mass, depress metabolism, create nutritional inadequacies, and cause greater weight gain in the future.\nHealth professionals around the world believe that a rapid weight loss program that encourages anything more than 8 pounds a month should not even be considered. Slow weight loss, 3-8 pounds a month, is much better for your heart and can help your body reset its "weight clock." Rapid weight loss can be extremely hard on our heart and organs, not to mention be a huge "shock" to the body. This "shock" can cause the weight that you rapidly lost to rapidly reappear (and then some) when you fall back into your "normal habits."
827356
Plasma consists of 90% water. Rest is plasma protein(7-9%) and the other rest is serum globulins,prothrombin,fibrinogen,enzymes,meneral ions(Na+,K+, Cl-, etc), amino acids,sugars,hormones,urea,vitamins,fatty acids.
709812
You can measure it in a number of ways depending on the protein.\n\n-- pH may vary directly with concentration\n-- optical rotation measurements may work for some\n-- adding a dye to the protein and reading on a colorimeter\n-- Another way would be to degrade or react the protein in solution and then to measure the byproducts of the degradation/reaction by something as simple as a titration
514614
What is albumin?\nAlbumin is a protein manufactured by the liver. \n\n\nWhat does albumin do?\nAlbumin performs many functions including maintaining the "osmotic pressure" that causes fluid to remain within the blood stream instead of leaking out into the tissues. \n\n\nWhat diseases cause albumin to be too low?\nLiver disease, kidney disease, and malnutrition are the major causes of low albumin. A diseased liver produces insufficient albumin. Diseased kidneys sometimes lose large amounts of albumin into the urine faster than the liver can produce it (this is termed nephrotic syndrome). In malnutrition there is not enough protein in the patient's diet for the liver to make new albumin from. \n\n\nWhat is a normal level of albumin?\nThe normal value depends on the laboratory running the test. Most labs consider roughly 3.5 to 5 grams per deciliter to be normal. \n\nWhat happens if it gets too low?\nIn a healthy person with normal nutrition, the liver will simply manufacture more and the level will normalize. If albumin gets very low swelling can occur in the ankles (edema) and fluid can begin to accumulte in the abdomen (ascites) and in the lungs (pulmonary edema). \n\nHow can you make the albumin higher?\nThe person must return to health. Therefore the underlying disorder must be corrected. If the disorder is cirrhosis of the liver, the only way to correct low albumin is generally to have a liver transplant. \n\n\nWhy does albumin fluctuate so much?\nAlbumin levels are also dependant on the state of hydration of the body. A person that is deficient of water ("dry") because of dehydration will have an artificially low albumin level. This returns to normal when the dehydration is corrected. Albumin fluctuates so widely because it is very sensitive to changes in hydration of the body.
163607
It depends. if you stop eating, the glucose stores in the muscle tissue and the the liver are metabolized first. Muscle atropphy (shrink) rapidly with non-use. Like fat muscle cells don't go away they shrink.  The specific question you asked is really quite involved as in part it depends on what kind of sick. If you have a fever or infection and do not eat at all your body need energy to mobilize your immune system and muscle metabolizes more quickly than fat, if you are not eating at all. fat metabolizes best when the body is mid-level aerobic for long periods, say 60-70% of VO2 max for several hours.  So, in general if you are way sick and bed bound your mucscles will atrophy and your body will metabolize the muscle, then the fat.
755323
Because the absorption of food is reduced due to the lessened time it has in the small intestine.  The shorter the intestine, the less the absorption.  The less the absorption, the fewer calories which are taken into the body.  The fewer the calories, the increased opportunity for weight loss.
314069
glomerulus in kidney keeps protein out of urine and probably the loop of Henle and possibly the bladder would be damaged if protein was found in large amounts.
1125242
Proteinuria\n\nHealthy kidneys take wastes out of the blood but leave in protein. Impaired kidneys may fail to separate the protein from the wastes. Proteinuria means protein in the urine, and it is a sign of poor kidney function. If your urine makes foam in the toilet, it may contain high levels of protein. Your doctor may test for protein using a dipstick in a small sample of your urine taken in the doctor's office. The color of the dipstick indicates the presence or absence of proteinuria. For a more precise measurement, you may need to collect urine for 24 hours.
855869
primary,secondary, tertiary,quaternary.\n\na change in ph results in a change in the concentration of OH and HYDROGEN ions.the high content of hydrogen ions make proteins to coagulate
933413
The body has to have a supply of amino acids for vital functions, so less vital stores of protein such as in muscles start to be broken down to supply more important functions. \n\nIf you have ever seen film or pictures of chronically starved/malnourished people then you will have noticed that their arms and legs are very wasted as much of the muscle will have been broken down to allow amino acids to be used in the function and repair of organs such as the brain, heart, liver etc. Organisms with impaired liver and/or kidney function tend to suffer from the same problems as these illnesses often suppress appetite.
373564
It denatures the hemoglobin protein within the blood cells, inactivating it and essentially killing the blood cells. That is why our bodies' pH is neutral, anywhere from 4.5 to 8.5, because an extremely high or low pH is very dangerous.
1137440
True!! If you don't eat proteins then your body won't receive things that your body needs in order to develop! Your body won't  develop and you'll have serious illness that can affect you bad! That's why I encouareg you to eat as much proteins as your body needs. Just like we buyt thing we need in order to survive, our body also needs proteins in order to continue running like a car does!
95429
COAGULATED PROTEIN. tHEY WILL ALSO GET REDISH WHEN THEY ARE TOO OLD TO EAT OR COOK. BACTERIAL DECAY DOES THE SAME THING
1176807
Sounds like somebody is working on a biochem lab. :) \n\nDenaturation lowers enzyme activity because it changes the shape of the protein. Heat disrupts the tertiary structure by breaking covalent, non-covalent and van der waals interations between side chains of the protein. Proteins must be in the right conformation in order to perform their functions correctly. When they are denatured substrates can no longer bind to the active site, key amino acids are no longer in the correct position. \n\npH affects enzyme activity in the following ways: 1-enzyme binding to the active site 2-catalytic activity 3-ionization of the substrate 4-variation of protein structure. This is because pH will change the ionization state of certain side chains. (H+ ions will interact with \n\nOptimum conditions for alpha amylase (ptyalin) from wikipedia.com:\n Optimum pH-5.6 - 6.9\n Room temperatue- 37 degrees Celsius
829925
acidity, radiation, heat, etc. destroy the protein component of enzyme, it's denaturation.