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DI a!? ayyyyyRyyyyyyyyyys in this group. Phosphoproteins are combinations with phosphorous-containing compounds other than nucleic acid or lecithin. Casein from milk and perhaps vitellin from egg yolk are assigned to this group. Chromoproteins are combinations of proteins and pigments. Hemoglobin combines an iron pyrrole complex with protein; ferritin is an iron compound found in the liver and spleen; catalase, peroxidase and cytochrome C are iron-rich enzymes which assist in biological oxidations; hemocyanin is a copper-containing compound found in lower invertebrates; laccase and tyrosinase are copper-containing enzymes important in biological oxidations; and chlorophyll is a chromoprotein containing magnesium. Lipoproteins are proteins combined with lipids. These occur in cell nuclei, blood, egg yolk, milk and elsewhere. These rather ill-defined complexes are present in the thromboplastic factor, some viruses and bacterial antigens. Derived proteins are hydrolysis products of larger proteins. Proteans are insoluble products resulting from hydrolysis with water alone, or assisted by dilute acids or enzymes. Myosan comes from myosin and edestan comes from edistin, for example. Metaproteans or infraproteans are derivatives obtained by hydrolysis in acids or alkalis. These are insoluble in neutral salt solutions. Examples are acid metaprotein or acid albuminate and alkali metaprotein or alkali albuminate. Coagulated proteins are insoluble products obtained by heat or alcohol. Proteoses are soluble in water and cannot be coagulated by heating, but they precipitate from saturated ammonium sulfate or zinc sulfate. Peptones are also soluble in water and not precipitated by heating and do not precipitate from ammonium sulfate. Some alkaloidal reagents such as phosphotungstic acid acid will precipitate them. Peptides are combinations of two or more amino acids with the amino acid joining at the amino group of another. Now, my question is which proteins are most likely to compete with Carbidopa/Ldopa for the "carriers" in our bloodstream, when we factor in such factors as the digestion times, the amino acids obtained and the recombinations required? If there is any interest, I will tabulate the amino acid content of some of these proteins. Maybe gelatin is good and casein is bad ? Patrick J. Martin<73121,[log in to unmask]> 69,9 medicating for 6 years ] ids are molecules utilized in plants and animals as building blocks for the manufacture of proteins. We digest proteins from plants and animals to obtain these amines and amino acids for reassembly into the proteins we need. Some of the amino acids such as Ldopa are decomposed further to obtain neurotransmitters such are our dearly beloved dopamine. The part of this biochemical cycle of interest to all of us is the transfer of Ldopa from our digestive tract to our blood to our brain for conversion to dopamine. The "carrier" molecules in our blood are limited in capacity so Ldopa must compete with some of the other amino acids from our digested proteins. If we limit our protein intake to 200 grams and our intake of Ldopa is 1 gram (or 1000 milligrams), the competition for transport is pretty intense. Carbidopa retards the conversion of Ldopa (and other amino acids) to dopamine (and other amines) in the blood before the Ldopa is transferred through the blood-brain barrier to our brain. The odds for the desired transfer are somewhat improved from this pessimistic scenario because there are more than 20 different amino acids derived from digested protein and all of these molecules are not competing for the same "carriers". Also, not all proteins are digested to their amino acids immediately in the digestive tract. There are numerous proteins to confuse our speculations. Native (or simple) proteins hydrolyze directly to the amino acids and/or their derivatives. Albumins are characterized by being soluble in water and coagulated by heat. Examples are egg albumin, serum albumin, lactalbumin from milk, and leucosin from wheat. Globulins are proteins that are insoluble in water and coagulated by heat; soluble in salt solutions and precipitated from salt solutions as the salt concentration is increased. Myosinogen from muscle, edestin from hemp seed, ovoglobulin from egg yolk, serum globulin, amandin from almonds, legumin from peas and excelsin from Brazil nuts are in this group. Glutelins are insoluble in neutral solvents but soluble in dilute acids or bases. Examples are glutenin from wheat and orzenin from rice. Prolamins or gliadins are a group of native proteins that are soluble in 70 to 80 percent alcohol and insoluble in water or absolute alcohol -- 95+percent. Gliaden from wheat, hordein from barley and zein from corn are in this group. Albuminoids or scleroproteins are insoluble in neutral solvents. Elastin from ligaments; collagen from hide, bone and cartilage; and keratin from horn are found in this group. Histones are soluble in water and insoluble in dilute ammonia. Solutions of other proteins precipitate histones. The precipitate thus formed is soluble in dilute acids. Globin is from hemoglobin, histone is found in thymus and scombrone is from mackerel. Protamines are simpler in structure than the proteins named above. This group is soluble in water; not coagulated by heat; precipitates other proteins from water solutions; has strong basic properties and forms stable salts with strong mineral acids. Salmine from salmon, sturine from sturgeon, scombrine from mackerel and cyprinine from carp have the characteristics of this group. Conjugated proteins consist of proteins chemically combined with other compounds. Nucleoproteins are combinations of one or more proteins with nucleic acid. Such are found in glandular tissue and in the germ of grains. Glycoproteins or glucoproteins are proteins combined with compounds containing a carbohydrate group. Mucin from saliva, osseomucoid from bone and tendomucoid from tendon are examplea yyyyyyyyyyyyyyyyyyyyyyyyyyyyyyyyyyyyyyyyyyyyyyyyyyyyyyyyyyyy