Purification of acidic Z protein from human liver

Summary Preparation of Z protein from human liver is described. Z protein consists of 2 forms which have different isoelectric points, pI 5.8 and pI 8.7, respectively. The acidic Z protein has a molecular weight of about 11,000 and has binding affinity for BSP using gel filtration.     

Purification of the glutamate decarboxylase from human brain]

A method of purifying the glutamate decarboxylase from human brain is described. The enzyme was purified 8 000 fold in regard to the initial homogenate and appears homogenous by electrophoresis, both in denaturing and non-denaturing conditions. The molecular weight of the native enzyme and its subunits indicate that GAD from human brain is formed by two similar if non identical polypeptide chains. The Km for glutamate and pyridoxal phosphate found for the human enzyme, respectively 1,2.10(-3) M and 0,13.10(-6) M, are close to the Km found for the Mouse enzyme.     

Purification of 2 succinic semi-aldehyde reductases from the human brain]

Two succinic semi-aldehyde reductases (A and B) have been purified to electrophoretic homogeneity. Enzyme A, which is a monomer of molecular weight 40,000 +/- 5,000 reduces a wide range of aldehydes and is inhibited by some barbiturates and certain anticonvulsants. Enzyme B, which is a dimer of molecular weight 80,000 +/- 10,000, is very specific for succinic semi-aldehyde and is not inhibited by the aforementioned compounds.     

Purification of plasminogen activator(s) from human seminal plasma

Summary Human seminal plasma contains an activator of plasminogen which was chromatographically purified. The molecular weight was determined to be 67,000.This study was supported by grants from the Swedish Medical Research Council (No. B75-17X-4523-01).     

Immunocytochemical labeling of human chromosomes by antibodies from human autoimmune serum]

Mitotic human chromosomes are successively irradiated by ultraviolet, incubated with serum from a patient showing systemic lupus erythematosus (S.L.E.), and antihuman Sheep serum conjugated with peroxidase. After revelation by diaminobenzidine (DAB) banding patterns are pointed out. The chromosome labelling is discussed in comparison with results obtained in other immunocytochemical experiments.     

Purification from human plasma of endogenous dodium transport inhibitor(s)

Summary Na⁺, K⁺-ATPase inhibitors extracted from plasma of healthy human subjects displaced³H-ouabain binding to human erythrocytes and inhibited the Na⁺ efflux catalyzed by the Na⁺, K⁺-pump and unexpectedly the Na⁺, K⁺-cotransport system without alteration of the Na⁺, Na⁺-exchange or the Na⁺ passive permeability. This suggests the presence in healthy human plasma of endogenous factors with ouabain-like and furosemide-like activities.Acknowledgments. We are indebted to Dr M. A. Devynck for her advice on chemical measurements and to Dr R. P. Garay for his help with flux measurements     

Purification from human plasma of endogenous sodium transport inhibitor(s)

Na+,K+-ATPase inhibitors extracted from plasma of healthy human subjects displaced 3H-ouabain binding to human erythrocytes and inhibited the Na+ efflux catalyzed by the Na+,K+-pump and unexpectedly the Na+,K+-cotransport system without alteration of the Na+,Na+-exchange or the Na+ passive permeability. This suggests the presence in healthy human plasma of endogenous factors with ouabain-like and furosemide-like activities.     

Purification and partial characterization of a human plasma α1-heteroglycan

Summary A heteroglycan was purified from human plasma and partially characterized in terms of its major properties. It is noteworthy that the carbohydrate content of this blood constituent is unusually high (75%).This study was supported by grants from the National Institutes of Health (GM-10374), US Public Health Service.     

Proposition of a reference serum for the immunochemical assay of human serum proteins]

Sera of healthy students (from Academy of Paris) aged between 18 and 30 years were collected with a view to routine clinical testing. 50 samples each representing the pooled sera of 400 individuals were investigated by evaluating 7 proteins for each pooled sample. Calculations of standard deviations showed that there existed a significant reproductibility of less than 2% for the population as a whole. These pooled sera representing 20 000 individual blood samples are proposed as a standard of human serum proteins.     

Non-paramagnetism of human serum proteins

Zusammenfassung Normale Serumproteine wurden mittels Elektromagnetophorese in Zellulose-Azetatgel ausgeführt, wobei keine Trennung der einzelnen Proteine erfolgte. Es stellte sich heraus, dass Serumproteine keine paramagnetischen Eigenschaften aufweisen.     

Chromatosomes are not produced from Tetrahymena chromatin by micrococcal nuclease digestion

The subnucleosomal organization of Tetrahymena chromatin, which has an unusual H1 histone, was investigated by NaCl extraction and micrococcal nuclease digestion of nuclei. It was found that Tetrahymena histone H1 is extracted with 0.35 M NaCl, whereas bovine thyroid H1 is not. Micrococcal nuclease digestion of Tetrahymena nuclei did not yield chromatosomes as a stable intermediate, whereas digestion of bovine thyroid nuclei did.     

Partial purification of components from fasting human blood serum which stimulate the forward migration of human spermatozoa

Summary Components from fasting human serum that could stimulate the forward migration of human spermatozoa were isolated by gel filtration on Sephadex G-25. The results suggest that these components may be used to enhance sperm forward migration and, hence, pregnancy rate in artificial insemination with husband's semen, (AIH) especially in cases where the sperm forward migration is not optimal.This work was supported by a grant from the World Health Organization.