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Prospective studies of pregnant women were performed to compare individual variations in the plasma concentration of sex hormone binding globulin (SHBG) and pregnancy zone protein (PZP) during pregnancy, and to elucidate the degree of co-variation between these oestrogen sensitive proteins during gestation. The plasma concentration of SHBG manifested continuous increase reaching a 12-fold peak at delivery. The increase of the protease inhibitor PZP paralleled that of SHBG reaching a peak with a 25-fold increase by the beginning of the third trimester. Then it started to decline, while that of SHBG continued to increase. The synthesis of the protease inhibitor may also continue to increase during late gestation but its elimination from the circulation may be accelerated when the syncytiotrophoblastic area in contact with the maternal blood approaches its maximum. The unusually wide individual variation of PZP concentrations in non-pregnant women was confirmed. However, the individual levels increased proportionally during the progress of pregnancy, and we may speak of low, medium and high reactors for PZP. One initial conclusion to be drawn from the present findings is that the value of the plasma PZP concentration can only be interpreted from a pathophysiologic point of view if the patient's baseline level is known.

Liquefaction of coagulated human semen was inhibited by o-phenanthroline; subsequent addition of Zn2+ reversed this inhibition, but not if the coagulum was repeatedly washed before Zn2+ was added. No liquefaction of the coagulum occurred when Fe2+ was added (in a 1:3 molar ratio to o-phenanthroline), and the gel repeatedly washed. This o-phenanthroline-depleted coagulum was liquefied by resuspended pellet from ultracentrifuged pooled seminal plasma. In denatured and reduced semen coagulate, we identified the 52 kDa, 71 kDa, and 76 kDa protein bands of the predominant seminal vesicle protein. The protein was not present in the supernatant after centrifugation of coagulated semen, and it was degraded to several minor basic proteins when semen liquefied. These findings imply that the predominant seminal vesicle protein functions as the structural protein of coagulated semen. In much the same way as in ejaculated semen, the 52 kDa, 71 kDa, and 76 kDa protein bands in seminal vesicle secretion collected postmortem were digested to minor basic proteins after incubating the secretion with resuspended pellet from ultracentrifuged seminal plasma. This pellet contained the membrane-bound succinyl(alanine)3-p-nitroanilide hydrolysing peptidase of prostatic origin which, like the liquefaction process, was active in the presence of EGTA, inhibited by non-chelated Zn2+, and inactivated by o-phenanthroline--an inactivation that was reversed by Zn2+.

15 patients with active RA were observed over a 3-month period after starting chloroquine treatment. Clinical condition, plasma levels of chloroquine and levels of 15 individual plasma proteins were checked monthly. Nine patients responded favourably to therapy, 6 failed to respond. The responders had lower initial CRP, orosomucoid and ceruloplasmin levels, whereas their IgA and IgM levels were slightly elevated. Significant reductions in the levels of CRP, haptoglobin, orosomucoid, fibrinogen and ceruloplasmin occurred in the responder group of patients. Alfa1-antitrypsin, antichymotrypsin C3 and C4 levels within the normal range were frequently encountered despite other clear-cut signs of activity. The chloroquine levels did not differ between responders and non-responders, the mean concentrations being 1.04 and 1.6 micromol/l respectively. This study has also demonstrated that in selected cases, despite active joint disease, all acute phase proteins may be normal. Finally, it was obvious that chloroquine, even when inducing remission, only brought about a partial normalization of the plasma protein pattern.

The predominant protein in human seminal vesicle secretion constitutes the structural protein of coagulated semen. This high molecular weight protein (HMW-SV-protein) is stable in seminal vesicle secretion during in vitro storage at 37 degrees C for at least 20 h, but is rapidly cleaved on mixing with prostatic proteases. Seminal coagulate, washed free of soluble components, is dissoluble by 2 to 3 mol/l of guanidine-HCl. Although dithiothreitol added to seminal coagulate does not liquefy the clot, complexes between HMW-SV-proteins are broken up by reduction under denaturing conditions, which suggests that the non-covalent linkages of HMW-SV-proteins are essential in the clot. Prostatic proteases cleave the HMW-SV-protein during liquefaction of ejaculated semen to a series of labile proteins. These proteins are further cleaved to peptides of successively decreasing size after completed liquefaction. The cleavage of the HMW-SV-protein is the major cause of the fast shift of the electrophoretic pattern of seminal proteins if semen is stored without protease inhibitors.

The authors report the concentration of some plasma proteins after administration of mestranol and/or chlormadinone in 19 controls and 43 women who had had recurrent cholestasis during previous pregnancies. Mestranol alone and combined with chlormadinone acetate induced enhanced βIC-globulin and fibrinogen and depressed cold insoluble globulin level. The changes were, if anything, more marked in women with cholestasis during an earlier pregnancy. No change of antichymotrypsin or C-reactive proteins was found in any of the groups. Chlormadinone acetate alone produced no apparent alterations in the plasma protein pattern.

A serum containing an M-component of IgM type gave on immunoelectrophoresis a biarcuate precipitation line. The anodal arch was produced by subunits of IgM, the other, by polymeric (17 S) IgM. The subunits combined in other optimal proportions with anti IgM than polymeric IgM as shown by e.g. immunoelectrophoresis and antigen-antibody crossed electrophoresis. Changes in immunoprecipitation patterns after reduction with mercaptoethanol of the cathodal arch to a mobility more equal to the anodal arch is one way to trace IgM subunits in plasma.

(1965). Electrophoretic Microheterogeneity of Serum α1-Antitrypsin. Scandinavian Journal of Clinical and Laboratory Investigation: Vol. 17, No. 3, pp. 271-274.

The response of 18 plasma proteins after cholecystectomy has been followed up for 3 weeks. The acute phase reaction has been compared with that after mastectomy. The response to these tissue lesions were very similar but more intense after cholecystectomy. The finding suggest that a2-macroglobulin may be used as an internal standard since no apparent changes appear. The concentration decreases during the first few postoperative days for albumin, α-lipoproteins, transferrin and prealbumin. No common cause is probable. C-reactive protein and antichymotrypsin begin to rise within eight hours. One day later orosomucoid, fibrinogen, haptoglobin and α1-antitrypsin show a strong reaction. Hemopexin, β1c-globulin, prothrombin, ceruloplasmin, Gc-globulin, α1, easily precipitable glycoprotein, plasminogen and cold insoluble globulin showed a delayed reaction with a moderate increase within a week. The immunoglobulins show insignificant changes.

The serum concentrations of α1-antitrypsin and α2-macroglobulin were determined immunochemicaHy in 50 cases with α1-antitrypsin deficiency. The mean α1-antitrypsin concentration was found to be 14.5 per cent and the mean α2-macroglobulin concentration 134 per cent of the normal concentration. No significant difference could be demonstrated between subjects with and without chronic lung disease. The trypsin inhibiting capacity of the inter-α trypsin inhibitor was estimated in two serum pools from subjects with and without pulmonary disease after separation of the serum inhibitors by gel filtration. It was found to be normal in both.

The main constituents of the a,-fraction obtained on paper electrophoresis in a barbital buffer are α1-lipoproteins, orosomucoid (acid glycoprotein), Schmid's (1953) and Schultze et al.'s α1-3.5 S ...

In a previous investigation it was observed that, on paper electrophoresis of serum with a barbital buffer containing calcium ions, part of the conventional 8-fraction migrated at a lower rate. This retarded part was called the &ca-fraction and the remainder the jlfraction. It was also found that when the serum was allowed to stand at room temperature before electrophoretic analysis this slow fraction decreased and was substantially smaller already within 24 hours. This reduction was tentatively ascribed to the assumption that the &ca-fraction contained some labile component(s) (Laurel1 et al. 1956). The publication of Muller-Eberhard & Nilsson (1960) on the /?,c-globulin and the spontaneous conversion of this protein to the electrophoretically faster /?,,-globulin gave us a clue to the nature of the labile p2Ca-fraction. We have since been able to identify the labile part of the electrophoretic B2Ca-fraction as /Ilc by comparative paper-, agar and imiiiunoelectroplioretic studies, and it was therefore possible to devise a simple analytical procedure for estimating the relative amount of the main normal components of the paper electrophoretic &ca-fraction (8lipoproteins and blc) in a given serum and for revealing any abnormal components with &-mobility.

The electrophoretic distribution of the 14 plasma components of decisive influence on the normal gel electrophoretic plasma patterns are presented. The genetic variants and aquired shifts in disease are outlined with comments on blurred and displaced bands as a result of intercation phenomenon of individual proteins. The common electrophoretic band patterns of cerebrospinal fluid and urine in health and disease are analysed.

Serum proteins of 30 women were estimated before, and 6 months after, regular intake of contraceptive pills (0.1 mg mestranol and 5 mg megestrol). A highly significant rise of increasing degree was observed for α2-macroglobulin, lipoproteins, transferrin, plasminogen, α1-antitrypsin, thyroxine-binding globulin (cortisol), and ceruloplasmin. The immunoglobulins were unchanged, but albumin, haptoglobins, and orosomucoid showed a highly significant decrease. The fall of orosomucoid and haptoglobins was greater than during pregnancy, while the rise of α1-antitrypsin, α2-macroglobulin, lipoproteins, and transferrin was less. It is concluded that the metabolic effects of contraceptive steroids has not been properly explored. This study implies that these metabolic effects are only in partial agreement with the alterations occurring during normal pregnancy.

D-Penicillamine treatment in rheumatoid arthritis resulted in a fall in plasma alfa-1-antitrypsin-IgA complexes which was significantly more pronounced among responders than among non-responders. Plasma free cystine levels also fell during D-penicillamine treatment, the fall being dose dependent up to a daily dose of 500 mg. Higher doses did not result in further lowering, and no difference was detected between responders and non responders. The dominating sulphur containing aminoacid excreted in the urine was penicillamine-cysteine disulphide, the concentration of which did not correlate to either toxicity or clinical effectiveness, but showed much individual variation. The slow kinetics of change in the complex concentration taken together with in vitro experiments, suggest that the effect of D-penicillamine is more likely to be on the de novo formation of the complexes, rather than on their reduction.

The normal ranges of variation of the acute phase reactants α1-antitrypsin, orosomucoid, haptoglobins and ceruloplasmin in maternal and fetal sera at delivery are given. The results suggest that rate of synthesis of α1-antitrypsin and orosomucoid calculated accord ing to bodyweight, is at least twice as high in the mother as in the fetus. The corresponding ratio for the other two proteins was still higher.

(1965). Effect of Neuraminidase, Acetone and Chloroform on α1-Antitrypsins. Scandinavian Journal of Clinical and Laboratory Investigation: Vol. 17, No. 3, pp. 297-298.