| D010776 |
Photobacterium |
A genus of gram-negative, facultatively anaerobic, rod-shaped bacteria that are common in the marine environment and on the surfaces and in the intestinal contents of marine animals. Some species are bioluminescent and are found as symbionts in specialized luminous organs of fish. |
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| 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 |
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| D013194 |
Staining and Labeling |
The marking of biological material with a dye or other reagent for the purpose of identifying and quantitating components of tissues, cells or their extracts. |
Histological Labeling,Staining,Histological Labelings,Labeling and Staining,Labeling, Histological,Labelings, Histological,Stainings |
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| D054788 |
Ribosome Inactivating Proteins |
N-Glycosidases that remove adenines from RIBOSOMAL RNA, depurinating the conserved alpha-sarcin loop of 28S RIBOSOMAL RNA. They often consist of a toxic A subunit and a binding lectin B subunit. They may be considered as PROTEIN SYNTHESIS INHIBITORS. They are found in many PLANTS and have cytotoxic and antiviral activity. |
RIP Ribosome Inactivating Proteins,RNA N-Glycosidase,Polynucleotide Adenosine Glycosidase,RIP (Ribosome Inactivating Proteins),RNA Glycosylase,rRNA N-Glycosylases,Adenosine Glycosidase, Polynucleotide,Glycosidase, Polynucleotide Adenosine,Glycosylase, RNA,Inactivating Proteins, Ribosome,N-Glycosidase, RNA,N-Glycosylases, rRNA,Proteins, Ribosome Inactivating,RNA N Glycosidase,rRNA N Glycosylases |
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| D019158 |
N-Acetylneuraminic Acid |
An N-acyl derivative of neuraminic acid. N-acetylneuraminic acid occurs in many polysaccharides, glycoproteins, and glycolipids in animals and bacteria. (From Dorland, 28th ed, p1518) |
Sialic Acid,Acid, N-Acetylneuraminic,Acid, Sialic,N Acetylneuraminic Acid |
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| D037121 |
Plant Lectins |
Protein or glycoprotein substances of plant origin that bind to sugar moieties in cell walls or membranes. Some carbohydrate-metabolizing proteins (ENZYMES) from PLANTS also bind to carbohydrates, however they are not considered lectins. Many plant lectins change the physiology of the membrane of BLOOD CELLS to cause agglutination, mitosis, or other biochemical changes. They may play a role in plant defense mechanisms. |
Lectins, Plant,Phytagglutinin,Plant Agglutinin,Plant Lectin,Agglutinins, Plant,Phytagglutinins,Plant Agglutinins,Agglutinin, Plant,Lectin, Plant |
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