Biomaterial Database

The isolation and partial characterization of alpha 2-macroglobulin from the serum of the ostrich (Struthio camelus. 1994

F Van Jaarsveld, and R J Naudé, and W Oelofsen, and J Travis

Department of Biochemistry, University of Port Elizabeth, South Africa.

1. alpha 2-Macroglobulin (alpha 2M) activity is present in the serum of the ostrich, Struthio camelus. The chromogenic synthetic peptide substrates BAPNA and ATNA were hydrolysed by trypsin and chymotrypsin, respectively, in the presence of ostrich serum and the alpha 2 M in ostrich serum protected trypsin from being inhibited by soybean trypsin inhibitor. Ostrich alpha 2M proved to be a potent inhibitor of bovine pancreatic trypsin and chymotrypsin. 2. alpha 2M was purified to apparent homogeneity by PEG precipitation, DEAE-Toyopearl 650M, Bio-Gel A-5m and Zn(2+)-affinity chromatography. 3. Ostrich alpha 2M migrated as a single band (M(r) 779,000 during non-denaturing gradient gel electrophoresis and showed increased mobility after reaction with trypsin. Denaturation dissociated ostrich alpha 2M into half-molecules. Denaturation with reduction further dissociated the protein into quarter-subunits. 4. Isoelectric focusing revealed a pI of 5.3. 5. The amino acid composition of ostrich alpha 2M is typical of an alpha 2M, comparing favourably with those of other animal species. The carbohydrate composition of the purified protein, in percentage dry weight of the molecule, was galactose: mannose (1:1), 4.55; N-acetylglucosamine 2.35; N-acetylneuraminic acid, 0.58; and fucose, 0.77. 6. alpha 2M was assessed immunologically by Ouchterlony double-diffusion and Western blot analysis with polyvalent antisera directed against ostrich alpha 2M. 7. Ostrich alpha 2M seems to show many physical, chemical and kinetic properties similar to those of other known alpha 2M(s), but is expected to differ from other alpha Ms when considering the primary structure of the bait region, the area differing among alpha Ms from different species and determining its specificity.

UI	MeSH Term	Description	Entries
D007448	Invertebrates	Animals that have no spinal column.	Brachiopoda,Mesozoa,Brachiopodas,Invertebrate,Mesozoas
D007700	Kinetics	The rate dynamics in chemical or physical systems.
D008969	Molecular Sequence Data	Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.	Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D000511	alpha-Macroglobulins	Glycoproteins with a molecular weight of approximately 620,000 to 680,000. Precipitation by electrophoresis is in the alpha region. They include alpha 1-macroglobulins and alpha 2-macroglobulins. These proteins exhibit trypsin-, chymotrypsin-, thrombin-, and plasmin-binding activity and function as hormonal transporters.	Slow alpha 2-Macroglobulins,alpha 2-Acute Phase Globulins,alpha-Macrofetoproteins,45S RNP,Acute-Phase alpha 1-Protein,Slow alpha 2-Globulin,alpha 1-Acute Phase Globulin,alpha 1-Acute Phase Protein,alpha 1-Macroglobulin,alpha 2-Acute Phase Globulin,alpha-Macrofetoprotein,Acute Phase alpha 1 Protein,RNP, 45S,Slow alpha 2 Globulin,Slow alpha 2 Macroglobulins,alpha 1 Acute Phase Globulin,alpha 1 Acute Phase Protein,alpha 1 Macroglobulin,alpha 1-Protein, Acute-Phase,alpha 2 Acute Phase Globulin,alpha 2 Acute Phase Globulins,alpha 2-Globulin, Slow,alpha 2-Macroglobulins, Slow,alpha Macrofetoprotein,alpha Macrofetoproteins,alpha Macroglobulins
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D001717	Birds	Warm-blooded VERTEBRATES possessing FEATHERS and belonging to the class Aves.	Aves,Bird
D013045	Species Specificity	The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.	Species Specificities,Specificities, Species,Specificity, Species
D014714	Vertebrates	Animals having a vertebral column, members of the phylum Chordata, subphylum Craniata comprising mammals, birds, reptiles, amphibians, and fishes.	Vertebrate
D016415	Sequence Alignment	The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.	Sequence Homology Determination,Determination, Sequence Homology,Alignment, Sequence,Alignments, Sequence,Determinations, Sequence Homology,Sequence Alignments,Sequence Homology Determinations