| D007074 |
Immunoglobulin G |
The major immunoglobulin isotype class in normal human serum. There are several isotype subclasses of IgG, for example, IgG1, IgG2A, and IgG2B. |
Gamma Globulin, 7S,IgG,IgG Antibody,Allerglobuline,IgG(T),IgG1,IgG2,IgG2A,IgG2B,IgG3,IgG4,Immunoglobulin GT,Polyglobin,7S Gamma Globulin,Antibody, IgG,GT, Immunoglobulin |
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| D007075 |
Immunoglobulin M |
A class of immunoglobulin bearing mu chains (IMMUNOGLOBULIN MU-CHAINS). IgM can fix COMPLEMENT. The name comes from its high molecular weight and originally was called a macroglobulin. |
Gamma Globulin, 19S,IgM,IgM Antibody,IgM1,IgM2,19S Gamma Globulin,Antibody, IgM |
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| D008855 |
Microscopy, Electron, Scanning |
Microscopy in which the object is examined directly by an electron beam scanning the specimen point-by-point. The image is constructed by detecting the products of specimen interactions that are projected above the plane of the sample, such as backscattered electrons. Although SCANNING TRANSMISSION ELECTRON MICROSCOPY also scans the specimen point by point with the electron beam, the image is constructed by detecting the electrons, or their interaction products that are transmitted through the sample plane, so that is a form of TRANSMISSION ELECTRON MICROSCOPY. |
Scanning Electron Microscopy,Electron Scanning Microscopy,Electron Microscopies, Scanning,Electron Microscopy, Scanning,Electron Scanning Microscopies,Microscopies, Electron Scanning,Microscopies, Scanning Electron,Microscopy, Electron Scanning,Microscopy, Scanning Electron,Scanning Electron Microscopies,Scanning Microscopies, Electron,Scanning Microscopy, Electron |
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| D005293 |
Ferritins |
Iron-containing proteins that are widely distributed in animals, plants, and microorganisms. Their major function is to store IRON in a nontoxic bioavailable form. Each ferritin molecule consists of ferric iron in a hollow protein shell (APOFERRITINS) made of 24 subunits of various sequences depending on the species and tissue types. |
Basic Isoferritin,Ferritin,Isoferritin,Isoferritin, Basic |
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| D006433 |
Hemocyanins |
Metalloproteins that function as oxygen transport proteins in the HEMOLYMPH of MOLLUSKS and ARTHROPODS. They are characterized by two copper atoms, coordinated with HISTIDINE residues, that reversibly bind a single oxygen molecule; they do not contain HEME groups. |
Hemocyanin,alpha-Haemocyanin,alpha-Hemocyanin,alpha-Hemocyanins,alpha Haemocyanin,alpha Hemocyanin,alpha Hemocyanins |
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| 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 |
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| D001052 |
Apoferritins |
The protein components of ferritins. Apoferritins are shell-like structures containing nanocavities and ferroxidase activities. Apoferritin shells are composed of 24 subunits, heteropolymers in vertebrates and homopolymers in bacteria. In vertebrates, there are two types of subunits, light chain and heavy chain. The heavy chain contains the ferroxidase activity. |
Apoferritin,Ferritin H Subunit,Ferritin Heavy Chain,Ferritin L Subunit,Ferritin Light Chain,H Ferritin,H-Ferritin,L-Ferritin,Ferritin, H,H Subunit, Ferritin,Heavy Chain, Ferritin,L Ferritin,L Subunit, Ferritin,Light Chain, Ferritin |
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| D046911 |
Macromolecular Substances |
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure. |
Macromolecular Complexes,Macromolecular Compounds,Macromolecular Compounds and Complexes,Complexes, Macromolecular,Compounds, Macromolecular,Substances, Macromolecular |
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