C.-B. Laurell

Sequential changes of plasma proteins after surgical trauma.

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.

Effect of administration of a combined estrogen-progestin contraceptive on the level of individual plasma proteins.

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.

Obstructive Lung Disease and Trypsin Inhibitors in α1-Antitrypsin Deficiency

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.

Composition and Variation of the Gel Electrophoretic Fractions of Plasma, Cerebrospinal Fluid and Urine

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.

The predominant protein in human seminal coagulate

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.

Plasma protein pattern in cirrhosis of the liver.

In 40 cases of liver cirrhosis in a quiescent state the plasma level of 21 proteins was determined. The acute phase reactants, haptoglobins and orosomucoid were normal or decreased, while α1-antitrypsin, fibrinogen and C-reactive protein were slightly increased or normal. Prealbumin, prothrombin and β2-glycoprotein I were most frequently subnormal. Of the plasma proteins studied prealbumin seemed to be the most sensitive indicator of the impaired liver function. The mean α2 -macroglobulin, IgA and IgG were doubled but in many cases the values were normal. a2-macroglobulin and albumin synthesized in the liver seemed to vary independently of each other also in hypoalbuminemia.

Sequential Changes of the Plasma Protein Pattern in Inoculation Hepatitis

22 plasma proteins were followed in inoculation hepatitis for two months after onset of icterus. Increased plasma ai-antitrypsin combined with normal orosomucoid and decreased haptoglobin level are charcteristic findings. The immunoglobulins show only insignificant changes. Abnormal complement activation seems to be uncommon. Low prealbumin and a-lipoprotein values are regular findings in periods with pronounced enzyme leakage from the liver. The immunologic reactivity of the a-Iipoproteins changes during the course of the disease.

Characterization of the predominant basic protein in human seminal plasma, one cleavage product of the major seminal vesicle protein

From liquefied human seminal plasma, we purified the predominant basic protein which appears following liquefaction of coagulated semen. The protein was purified in the presence of di-isopropylfluorophosphate to retard its degradation. Heparin-Sepharose chromatography was followed by gel filtration (Biogel P 60) and by fast performance liquid chromatography on a reversed phase column (C8). The basic protein is a single polypeptide chain with an apparent molecular mass of 12.8 kDa, and has a pI value between that of trypsinogen (9.3) and cytochrome C (10.3). The protein contains no carbohydrate, is rich in histidine, glutamate, and lysine, but is devoid of both cysteine and methionine. The amino-terminal portion of the protein sequence is unique: H N K Q E G R D H D K S K G H F H R V V I H H K G G K A H R G-. A specific rabbit antiserum was raised against the 12.8 kDa basic protein. The protein was found to be unique to seminal plasma among all extracellular fluids examined. Three immunologically related 52 kDa, 71 kDa, and 76 kDa proteins were identified in seminal vesicle secretion when it had been reduced. Prostatic enzyme(s) degraded these proteins to the 12.8 kDa basic protein and several other basic proteins with apparent molecular masses below 18 kDa.

Disorders of Serum α-Lipoproteins after Alcoholic Intoxication

Increased levels of serum α-lipoproteins were detected in about 30 per cent of alcoholics submitted for medical care. Abnormal electrophoretic distribution of the α-lipoproteins was common in these cases.

Orosomucoid and α1-antitrypsin in Maternal and Fetal Sera at Parturition

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.