1. The analysis, by silica-gel chromatography, of phospholipids from a human-plasma fraction is described. The fraction was derived from whole blood which had been incubated with sodium [Me-14C]acetate for 6-5 hr. The #-lipoproteins had been removed by precipitation with dextran sulphate. 2. All the phospholipids isolated were labelled. 3. The fatty acids of the isolated phospholipids were analysed by vapour-phase chromatography. 4. A comparison of yield, radioactivity and fatty acid distribution with those for the phospholipids of the cells is given.

Metabolic heterogeneity of human γ-globulin

Publisher Summary This chapter discusses metabolism of plasma proteins. The metabolism of plasma proteins is a specific example of protein turnover. Superficially, the phenomena associated with this kind of turnover appear to be relatively simple and readily amenable to experimental verification because of the accessibility of the proteins involved. It is a great advantage that the newly synthesized plasma proteins pass quickly out of the cells in which they are made and are delivered into a large and relatively stable plasma pool. There is one major qualification to this that arises from the existence of an extravascular pool of similar proteins usually comparable in size to the intravascular one. The presence of such a pool is immediately evident in the way in which a labeled protein is eliminated from the plasma in the few days immediately following its injection. The site of catabolism of plasma proteins is not precisely known, although the following indirect evidence indicates that it must be in close proximity functionally to the plasma.

Metabolism of Plasma Proteins

Turnovers of Erythrocytes and Plasma Proteins in Mammals

Publisher Summary This chapter describes three variants of serum albumin: (1) the permanent presence of an unusual albumin in the body fluids (hereditary alloalbuminernia), (2) its temporary appearance (transient bisalbuminemia), and (3) the near absence of any albumin at all (analbuminemia). The three types of albumin abnormality affect methods of protein analysis, setting diagnostic puzzles, especially in countries where alloalbuminemia is rare and the error in the laboratory result goes unnoticed. The use of techniques for finding cases of alloalbuminemia and for characterizing the variants in order to build up some system of classification has been presented in the chapter. Classification has been attempted in two ways: by Weitkamp's system of starch gel electrophoresis at three pH levels and by the test schedule of the Royal Berkshire Hospital. Drug-induced bisalbuminemia has been turned into a bacteriological test, and the hereditary type has had two laboratory applications: Phillips et al. have used the bisalbuminemic serum from chicken-turkey hybrids as a model for comparing methods of protein separation, and the Italian Committee for Standardization of Laboratory Methods first became interested in bisalbuminemia as quality control material for checking the efficiency of electrophoretic separations.

Genetic and Drug-Induced Variation in Serum Albumin

The normal regulation of intravascular plasma protein mass has not been fully investigated. It has long been known that plasma proteins rapidly return to normal concentrations after plasmapheresis, but the means by which this takes place has not been clearly demonstrated. In pathological states, such as nephrosis and hypercatabolic hypoproteinemia, where there may be a steady loss of plasma protein, some compensatory mechanism (see next paragraph) must be involved in cases in which the intravascular plasma proteins are in a steady state. Frequently the protein concentration alone is determined, so that it is not known whether changes are due to variations in plasma volume or in total intravascular protein mass. A steady state can only be said to exist when the plasma protein synthesized is equal to that catabolized, so that the total mass of protein, but not necessarily the concentration, is constant. Disturbances of intravascular protein mass could be compensated for by a) change in synthesis rate, b) change in catabolic rate, c) net transfer of protein between extravascular and intravascular protein pools or d) a combination of several of these. There is also the possibility that the proportion of the different protein fractions is altered and that loss of one fraction is replaced by an increase of another fraction. The purpose of this investigation was to obtain further evidence on this problem by removing protein by plasmapheresis and observing the effect on the catabolic rate, intravascular pool mass, concentration and volume, and on the sum of synthesis rate plus net transfer rate from extravascular to intravascular pool. Rabbits on a normal diet were used, and a single protein fraction, albumin, was considered. I131-rabbit albumin was injected intravenously into rabbits, and plasma albumin specific activity (microcuries per gram), total body radioactivity

/pdf/effects-of-plasmapheresis-on-albumin-pools-in-rabbits-331156a50x.pdf

Effects of plasmapheresis on albumin pools in rabbits.

THE behaviour of plasma proteins labelled with iodine-131 in the circulation of animals has been shown1–3 to correspond with that of the same proteins biosynthetically labelled with carbon-14, supporting the view that the iodine label, if properly applied, may be a reliable indicator of the behaviour of unlabelled molecules.

Albumin labelled with iodine-131 in an analbuminaemic subject.

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Albumin labelled with iodine-131 in an analbuminaemic subject.