Hemolysins: pore-forming proteins in invertebrates
Invertebrates possess lytic molecules which lyse vertebrate erythrocytes. In all the species studied so far, hemolytic activity depends on proteins which possess a wide range of reactivity. It is generally calcium-dependent and heat-labile, although calcium-independent and heat-stable hemolysins hav...
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| Veröffentlicht in: | Experientia 1990-03, Vol.46 (3), p.239-244 |
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| creator | CANICATTI, C |
| description | Invertebrates possess lytic molecules which lyse vertebrate erythrocytes. In all the species studied so far, hemolytic activity depends on proteins which possess a wide range of reactivity. It is generally calcium-dependent and heat-labile, although calcium-independent and heat-stable hemolysins have also been detected. The molecules interact with sugars or lipids which could represent the membrane receptors by which circular lesions on target membranes are produced. On the basis of some analogies with vertebrate lytic molecules it is conceivable that the hemolysins evolved from a common ancestral gene which also led to vertebrate pore-forming proteins. |
| doi_str_mv | 10.1007/BF01951753 |
| format | Article |
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In all the species studied so far, hemolytic activity depends on proteins which possess a wide range of reactivity. It is generally calcium-dependent and heat-labile, although calcium-independent and heat-stable hemolysins have also been detected. The molecules interact with sugars or lipids which could represent the membrane receptors by which circular lesions on target membranes are produced. On the basis of some analogies with vertebrate lytic molecules it is conceivable that the hemolysins evolved from a common ancestral gene which also led to vertebrate pore-forming proteins.</description><identifier>ISSN: 0014-4754</identifier><identifier>EISSN: 1420-9071</identifier><identifier>DOI: 10.1007/BF01951753</identifier><identifier>PMID: 2178952</identifier><identifier>CODEN: EXPEAM</identifier><language>eng</language><publisher>Basel: Birkhäuser</publisher><subject>Animals ; Biological and medical sciences ; Calcium - metabolism ; Erythrocyte Membrane - pathology ; Fundamental and applied biological sciences. Psychology ; General aspects ; General aspects and techniques. Study of several systematic groups. 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In all the species studied so far, hemolytic activity depends on proteins which possess a wide range of reactivity. It is generally calcium-dependent and heat-labile, although calcium-independent and heat-stable hemolysins have also been detected. The molecules interact with sugars or lipids which could represent the membrane receptors by which circular lesions on target membranes are produced. On the basis of some analogies with vertebrate lytic molecules it is conceivable that the hemolysins evolved from a common ancestral gene which also led to vertebrate pore-forming proteins.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Calcium - metabolism</subject><subject>Erythrocyte Membrane - pathology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General aspects</subject><subject>General aspects and techniques. Study of several systematic groups. Models</subject><subject>Hemolysin Proteins - metabolism</subject><subject>Hemolysin Proteins - pharmacology</subject><subject>Hemolysin Proteins - physiology</subject><subject>Hemolysis</subject><subject>Invertebrata</subject><subject>Invertebrates</subject><subject>Invertebrates - immunology</subject><subject>Invertebrates - metabolism</subject><subject>Kinetics</subject><subject>Magnesium - metabolism</subject><subject>Marine</subject><subject>Proteins - metabolism</subject><subject>Proteins - pharmacology</subject><subject>Proteins - physiology</subject><subject>Rabbits</subject><issn>0014-4754</issn><issn>1420-9071</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkM1Lw0AQxRdRaq1evAs9iAchOpP99laLtULBi57DZjuRSD7qbir0vzfSUI_CwMC8H28ej7FLhDsE0PePC0ArUUt-xMYoUkgsaDxmYwAUidBSnLKzGD8BOEhUIzZKURsr0zFLl1S31S6WTXyYbtpASdGGumw-ppvQdtSfp2XTzzeFjvLgOorn7KRwVaSLYU_Y--Lpbb5MVq_PL_PZKvFcpF1SgBRIqUBpiCRKwcnyteHKSW20zwuhhELhc45eeaO1BF9o4XluvUVt-YTd7H37JF9bil1Wl9FTVbmG2m3MtFVSc23-BfvfylojevB2D_rQxhioyDahrF3YZQjZb5PZX5M9fDW4bvOa1gd0qK7XrwfdRe-qIrjGl_GAKSOUssB_AICceF4</recordid><startdate>19900315</startdate><enddate>19900315</enddate><creator>CANICATTI, C</creator><general>Birkhäuser</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>7X8</scope></search><sort><creationdate>19900315</creationdate><title>Hemolysins: pore-forming proteins in invertebrates</title><author>CANICATTI, C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c342t-f0541e24158ee51543e93d836a5787cbf464614cb31c6c87750cf74c3b9c91793</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Calcium - metabolism</topic><topic>Erythrocyte Membrane - pathology</topic><topic>Fundamental and applied biological sciences. 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In all the species studied so far, hemolytic activity depends on proteins which possess a wide range of reactivity. It is generally calcium-dependent and heat-labile, although calcium-independent and heat-stable hemolysins have also been detected. The molecules interact with sugars or lipids which could represent the membrane receptors by which circular lesions on target membranes are produced. On the basis of some analogies with vertebrate lytic molecules it is conceivable that the hemolysins evolved from a common ancestral gene which also led to vertebrate pore-forming proteins.</abstract><cop>Basel</cop><cop>Boston, MA</cop><cop>Berlin</cop><pub>Birkhäuser</pub><pmid>2178952</pmid><doi>10.1007/BF01951753</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Experientia, 1990-03, Vol.46 (3), p.239-244 |
| issn | 0014-4754 1420-9071 |
| language | eng |
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| source | MEDLINE; SpringerLink Journals |
| subjects | Animals Biological and medical sciences Calcium - metabolism Erythrocyte Membrane - pathology Fundamental and applied biological sciences. Psychology General aspects General aspects and techniques. Study of several systematic groups. Models Hemolysin Proteins - metabolism Hemolysin Proteins - pharmacology Hemolysin Proteins - physiology Hemolysis Invertebrata Invertebrates Invertebrates - immunology Invertebrates - metabolism Kinetics Magnesium - metabolism Marine Proteins - metabolism Proteins - pharmacology Proteins - physiology Rabbits |
| title | Hemolysins: pore-forming proteins in invertebrates |
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