Or Globulins

The diversity in primary, secondary, tertiary, and quaternary stmctures of proteins means that few generalisations can be made concerning their chemical properties. Some fulfil stmctural roles, such as the collagens (found in bone) and keratin (found in claws and beaks), and are insoluble in all solvents. Others, such as albumins or globulins of plasma, are very soluble in water. Still others, which form part of membranes of cells, are partly hydrophilic ( water-loving , hence water-soluble) and partly lipophilic ( lipid-loving , hence fat-soluble). 

An interesting possible method to producing antibodies from serum or globulin solution outside of the animal is suggested by the theory. The globulin would be... 

Dialyze 1 ml of the serum or globulin solution against PBS overnight at 4°. 

Some medication particles bind to albumin or globulin protein in plasma, forming a medication-protein complex. Medication-protein complexes decrease the concentration of free medication in circulation because... 

Altered concentration of albumin or globulins Abnormal proteins Heparin pH ... 

Hypoproteinemias are characterized by reductions in albumin and/or globulin fractions reductions of albumin may be due to reduced hepatic synthesis or increased losses via the kidney or intestinal mucosa and several other tissues. Severe hypoproteinemia can be associated with edema and ascites due to the major osmotic influence of albumin. Some compounds, such as colchicines and cycloheximide, can... 

Once absorbed, dmg particles are transported in blood plasma. These are referred to as free dmgs because they are not bound to any receptor sites. Only free dmgs can cause a pharmacological response. Dmgs bind to proteins in plasma, usually albumin or globulins. These dmg-protein complexes decrease the concentration of free dmg in the circulation. This protein-dmg molecule is too large to pass through the membrane of a blood vessel and is not available for... 

To summarize, the final products of peptic digestion are composed of deutero-albumose C, products not precipitable by phosphotungstic acid, and peptones. The different results which have just been set forth relate to serum-albumin. Zunz has found that egg-albumin, casein or globulin, treated in a similar way, act in a similar manner. Yet the progress of digestion of these various materials does not show entirely the same course. In general, extensive hydrolysis is reached with these bodies with more difficulty than with serum-albumin. 

Proteins. Almeida (1948) has used a polarograph to identify certain proteins. From the similarity of the curves obtained with the extract of a port wine and pure solutions of albumins or globulins, he was able to estimate the protein content. A port wine deposit showed a relatively high protein content. He did not find peptones. 

Figure 3. Effect of globulins from sera of control and of immunized rabbits on cathepsin D activity in high-speed extracts of rat liver and of rat TDL. High-speed extracts of rat liver and of rat TDL were preincubated with control globulins from unimmunized rabbits (o) or globulins from antisera of rabbits immunized against soluble rat liver lysosomal enzymes ( ) for 1 hr at 370. Enzyme activity was measured at pH 5.0 according to the description of Yago and Bowers (5). Reproduced with permission from the Journal of Biological Chemistry.

Heat-coagulation will not take place in an alkaline solution, or in a strongly acid solution deficient in salts. Hence, in testing for albumin or globulin the solution is first slightly acidified with dilute acetic acid, and treated with sodium chloride. The coagulation temperature depends on the nature of the protein, the reaction of the mixture, and the electrolytes present. 

Acidify 5 ml. of solution with 1-3 drops of 20 per cent, acetic acid. Add a drop of 6-10 per cent, sodium chloride. Boil gently. A white coagulum shows the presence of albumin or globulin. This test is of special importance in the detection of these proteins in urine. 

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