| 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 |
|
| D011485 |
Protein Binding |
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. |
Plasma Protein Binding Capacity,Binding, Protein |
|
| D003030 |
Coagulase |
Enzymes that cause coagulation in plasma by forming a complex with human PROTHROMBIN. Coagulases are produced by certain STAPHYLOCOCCUS and YERSINIA PESTIS. Staphylococci produce two types of coagulase: Staphylocoagulase, a free coagulase that produces true clotting of plasma, and Staphylococcal clumping factor, a bound coagulase in the cell wall that induces clumping of cells in the presence of fibrinogen. |
Staphylocoagulase,Staphylococcal Clumping Factor,Clumping Factor (Staphylococcal),Staphylococcus aureus clone pSCa2 of Coagulase,Staphylococcus aureus strain 213 of Coagulase,Staphylococcus aureus strain 8325-4 of Coagulase,Clumping Factor, Staphylococcal,Factor, Staphylococcal Clumping,Staphylococcus aureus strain 8325 4 of Coagulase |
|
| D003179 |
Complement C3b |
The larger fragment generated from the cleavage of COMPLEMENT C3 by C3 CONVERTASE. It is a constituent of the ALTERNATIVE PATHWAY C3 CONVERTASE (C3bBb), and COMPLEMENT C5 CONVERTASES in both the classical (C4b2a3b) and the alternative (C3bBb3b) pathway. C3b participates in IMMUNE ADHERENCE REACTION and enhances PHAGOCYTOSIS. It can be inactivated (iC3b) or cleaved by various proteases to yield fragments such as COMPLEMENT C3C; COMPLEMENT C3D; C3e; C3f; and C3g. |
C3b Complement,C3bi,Complement 3b,Complement Component 3b,Inactivated C3b,iC3b,C3b, Complement,C3b, Inactivated,Complement, C3b,Component 3b, Complement |
|
| D006801 |
Humans |
Members of the species Homo sapiens. |
Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man |
|
| 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 |
|
| D013211 |
Staphylococcus aureus |
Potentially pathogenic bacteria found in nasal membranes, skin, hair follicles, and perineum of warm-blooded animals. They may cause a wide range of infections and intoxications. |
|
|
| D017244 |
Complement Factor I |
A plasma serine proteinase that cleaves the alpha-chains of C3b and C4b in the presence of the cofactors COMPLEMENT FACTOR H and C4-binding protein, respectively. It is a 66-kDa glycoprotein that converts C3b to inactivated C3b (iC3b) followed by the release of two fragments, C3c (150-kDa) and C3dg (41-kDa). It was formerly called KAF, C3bINF, or enzyme 3b inactivator. |
C3b Inactivator,C3b-C4b Inactivator,C4b-C3b-INA,C4bC3bINA,Complement 3b-Complement 4b Inactivator,Complement C4b-C3b Inactivator,C3b C4b Inactivator,C4b C3b INA,C4b-C3b Inactivator, Complement,Complement 3b Complement 4b Inactivator,Complement C4b C3b Inactivator,Inactivator, C3b,Inactivator, C3b-C4b,Inactivator, Complement C4b-C3b |
|
-transparent.png){kind=logo}
