Preparation and partial structural characterization of alpha1T-glycoprotein from normal human plasma.

alpha1T-glycoprotein (alpha1T) was isolated from normal human plasma in the immunochemically homogeneous state. The partial amino acid sequence and carbohydrate chains of this glycoprotein were determined. To achieve this, the carboxymethylated alpha1T was analyzed by sequencing some of the lysylendoprotease, V8 protease, tryptic, and cyanogen bromide peptides as well as the N-terminal sequence of the protein.

The effect of the carbohydrate moiety upon the size and conformation of human plasma galactoglycoprotein as judged by electron microscopy and circular dichroism. Structural studies of a glycoprotein after stepwise enzymic carbohydrate removal.

Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol. Chem.

[Poliomyelitis in Landsteiner's time and today].

At a meeting of the Royal and Imperial Association of Physicians in Vienna on December 18, 1908 Dr. Karl Landsteiner reported on the successful experimental transmission of poliomyelitis from man to ape in a study which he undertook together with Erwin Popper. In a scientific article that was published shortly after the meeting, Landsteiner wrote that "the poliomyelitis virus belongs to the group of filterable micro-organisms".

[Clinical importance of human plasma proteins and their future development].

For more than 50 years now, proteins based on human blood plasma are used as drugs. More than 20 different protein preparations: Albumin, immunoglobulins, coagulation factors and inhibitors are currently available for substitution therapy. In the near future, antihemophilic globulins and perhaps Factor IX, too, will be produced by genetic engineering, independent from human blood plasma.

Complete amino acid sequence of human plasma Zn-alpha 2-glycoprotein and its homology to histocompatibility antigens.

In the present study the complete amino acid sequence of human plasma Zn-alpha 2-glycoprotein was determined. This protein whose biological function is unknown consists of a single polypeptide chain of 276 amino acid residues including 8 tryptophan residues and has a pyroglutamyl residue at the amino terminus. The location of the two disulfide bonds in the polypeptide chain was also established.

Properties of acute phase proteins of human plasma.

Almost 50 years ago the term acute phase serum was used for the first time by Avery and his colleagues to characterize serum from patients in an acute state with inflammatory diseases and which contained C-reactive protein. In the meantime a variety of proteins was detected in human blood plasma which are subject to the acute phase response. About a fifth of the until today more than hundred isolated and well characterized plasma proteins are to be classified as acute phase proteins.

The structure of the carbohydrate units of human plasma galactoglycoprotein determined by 500-megahertz 1H NMR spectroscopy.

Human plasma galactoglycoprotein (Mr = 81,000) which was recently identified and characterized (Schmid, K., Mao, S. K.

Purified human plasma proteins of unknown function.

The development of new analytic and preparative techniques in the field of protein chemistry has essentially extended our knowledge about the variety of human plasma proteins in the last 15 years. In many cases plasma proteins have been particularly determined by immunologic techniques, partially highly purified and physicochemically well characterized, before knowing the biological function. To these proteins belong among others the alpha 1-antitrypsin, Cl-inactivator, alpha 2-macroglobulin, Gc-globulin and the cold-insoluble globulin.

C-reactive protein (CRP), 9.5 salpha1-glycoprotein and C1q: serum proteins with lectin properties?

The human serum proteins C-reactive protein (CRP), the 9.5 Salpha1-glycoprotein and C1q show, when tested in the agar gel diffusion under certain buffer conditions, strong precipitin reactions with polysaccharides of the galactan type, indicating that they may have lectin-like recognition sites.

Additional precipitation reactions of lectins with human serum glycoproteins.

Highly purified human serum glycoproteins were treated with neuraminidase and examined for their cross reaction with several lectins with anti-galactosyl specificity: beta-D-galactosyl structures are thought to be the main terminal sugar residues that become attached de novo after removal of neuraminic acid. The following lectins were tested: Tridacnin from the bivalve clams Tridacna maxima and Tridacna gigas, the agglutinin from the sponge Axinella polypoides, the lectin from the roach Rutilus rutilus and the plant lectins from Ricinus communis, Ononis spinosa, Glycine soja and Abrus precatorius. In agar gel diffusion, these purified and precipitating lectins gave more or less strong or negative results against the different neuraminidase-treated serum glycoproteins, thus indicating subtle differences with respect to their anti-galactosyl combining specificity.

Neuraminidase and tumor immunotherapy.

Preliminary results of first clinical studies with the enzyme neuraminidase call attention to a new kind of cancer treatment. This promising approach to tumor immunotherapy was entered into the clinical phase as a consequence of successful experimental studies in tumor-bearing mice, rats and dogs. In this review, the presently known and essential results of experimental and clinical studies on tumor immunotherapy by means of neuraminidase are presented as well as some necessary and critical considerations in this context.

A new marker for neuraminidase-treated human serum glycoproteins from the haemolymph of Tridacna maxima (Röding).

Highly purified human serum glycoproteins were treated with neuraminidase. The exposed subterminal carbohydrate structures reacted strongly with an anti-galactan precipitin from the haemolymph of Tridacna maxima which detects terminal, non-reducing beta-D-galactoside residues. This invertebrate precipitin, Tridacnin, may be used as a marker for nearly two thirds of all asialo serum glycoproteins; A number of different cross-reactions with various other polysaccharides and galactans subdivides those neuraminidase-treated glycoproteins into several subgroups, indicating that the uncovered carbohydrate structures are not always completely identical.