PubMed:6786352 JSONTXT

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":18,"end":25},"obj":"Cell"},{"id":"T2","span":{"begin":119,"end":126},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0003025"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0003025"}],"text":"Modulation of the epsilon-(gamma-glutamic)lysine cross-link in cellular proteins. I. In vivo and in vitro studies.\nThe epsilon-(gamma-glutamic)lysine cross-link content of intracellular proteins in a variety of cell types can be modulated in vivo by temperature changes and in vitro by treatment with Mg2+/-ATP and Mg2+/-ATP plus Ca2+. Virtually all the cross-links are found in the cytoskeletal and membrane components which are not solubilized by glycerol extraction. In the slime mold, Physarum polycephalum, enzyme activities persist which bring about a decrease in cross-link content upon addition of Mg2+/-ATP and an increase in cross-link content upon addition of Mg2+/-ATP plus Ca2+. In cultured embryonic chick skeletal myofibrils, we have observed a decrease in cross-link content upon addition of Mg2+/-ATP. In cultured embryonic chick heart myofibrils, we have observed an increase in cross-link content upon addition of Mg2+/-ATP followed by Ca2+. A hypothesis is discussed in which the modulation of Glu-Lys cross-links is explained in terms of a cycle of reactions which involves (1) the formation of an acyl phosphate of a glutamic acid side chain; (2) the formation of a Glu-Lys cross-link, and (3) the hydrolytic or phosphorylitic breakdown of the cross-links. In such a hypothesis, the role of Mg2+/-ATP is that of introducing energy which can be used for the cycling of cross-links and possibly for some cellular energy transductions."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":847,"end":852},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000036"}],"text":"Modulation of the epsilon-(gamma-glutamic)lysine cross-link in cellular proteins. I. In vivo and in vitro studies.\nThe epsilon-(gamma-glutamic)lysine cross-link content of intracellular proteins in a variety of cell types can be modulated in vivo by temperature changes and in vitro by treatment with Mg2+/-ATP and Mg2+/-ATP plus Ca2+. Virtually all the cross-links are found in the cytoskeletal and membrane components which are not solubilized by glycerol extraction. In the slime mold, Physarum polycephalum, enzyme activities persist which bring about a decrease in cross-link content upon addition of Mg2+/-ATP and an increase in cross-link content upon addition of Mg2+/-ATP plus Ca2+. In cultured embryonic chick skeletal myofibrils, we have observed a decrease in cross-link content upon addition of Mg2+/-ATP. In cultured embryonic chick heart myofibrils, we have observed an increase in cross-link content upon addition of Mg2+/-ATP followed by Ca2+. A hypothesis is discussed in which the modulation of Glu-Lys cross-links is explained in terms of a cycle of reactions which involves (1) the formation of an acyl phosphate of a glutamic acid side chain; (2) the formation of a Glu-Lys cross-link, and (3) the hydrolytic or phosphorylitic breakdown of the cross-links. In such a hypothesis, the role of Mg2+/-ATP is that of introducing energy which can be used for the cycling of cross-links and possibly for some cellular energy transductions."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":489,"end":510},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"5791"}],"text":"Modulation of the epsilon-(gamma-glutamic)lysine cross-link in cellular proteins. I. In vivo and in vitro studies.\nThe epsilon-(gamma-glutamic)lysine cross-link content of intracellular proteins in a variety of cell types can be modulated in vivo by temperature changes and in vitro by treatment with Mg2+/-ATP and Mg2+/-ATP plus Ca2+. Virtually all the cross-links are found in the cytoskeletal and membrane components which are not solubilized by glycerol extraction. In the slime mold, Physarum polycephalum, enzyme activities persist which bring about a decrease in cross-link content upon addition of Mg2+/-ATP and an increase in cross-link content upon addition of Mg2+/-ATP plus Ca2+. In cultured embryonic chick skeletal myofibrils, we have observed a decrease in cross-link content upon addition of Mg2+/-ATP. In cultured embryonic chick heart myofibrils, we have observed an increase in cross-link content upon addition of Mg2+/-ATP followed by Ca2+. A hypothesis is discussed in which the modulation of Glu-Lys cross-links is explained in terms of a cycle of reactions which involves (1) the formation of an acyl phosphate of a glutamic acid side chain; (2) the formation of a Glu-Lys cross-link, and (3) the hydrolytic or phosphorylitic breakdown of the cross-links. In such a hypothesis, the role of Mg2+/-ATP is that of introducing energy which can be used for the cycling of cross-links and possibly for some cellular energy transductions."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":172,"end":185},"obj":"Body_part"},{"id":"T2","span":{"begin":400,"end":408},"obj":"Body_part"},{"id":"T5","span":{"begin":729,"end":739},"obj":"Body_part"},{"id":"T6","span":{"begin":847,"end":852},"obj":"Body_part"},{"id":"T10","span":{"begin":853,"end":863},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/GO_0005622"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"A3","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0000094"},{"id":"A4","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/GO_0030016"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0000948"},{"id":"A7","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0007100"},{"id":"A8","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0015228"},{"id":"A9","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0015230"},{"id":"A10","pred":"uberon_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/GO_0030016"}],"text":"Modulation of the epsilon-(gamma-glutamic)lysine cross-link in cellular proteins. I. In vivo and in vitro studies.\nThe epsilon-(gamma-glutamic)lysine cross-link content of intracellular proteins in a variety of cell types can be modulated in vivo by temperature changes and in vitro by treatment with Mg2+/-ATP and Mg2+/-ATP plus Ca2+. Virtually all the cross-links are found in the cytoskeletal and membrane components which are not solubilized by glycerol extraction. In the slime mold, Physarum polycephalum, enzyme activities persist which bring about a decrease in cross-link content upon addition of Mg2+/-ATP and an increase in cross-link content upon addition of Mg2+/-ATP plus Ca2+. In cultured embryonic chick skeletal myofibrils, we have observed a decrease in cross-link content upon addition of Mg2+/-ATP. In cultured embryonic chick heart myofibrils, we have observed an increase in cross-link content upon addition of Mg2+/-ATP followed by Ca2+. A hypothesis is discussed in which the modulation of Glu-Lys cross-links is explained in terms of a cycle of reactions which involves (1) the formation of an acyl phosphate of a glutamic acid side chain; (2) the formation of a Glu-Lys cross-link, and (3) the hydrolytic or phosphorylitic breakdown of the cross-links. In such a hypothesis, the role of Mg2+/-ATP is that of introducing energy which can be used for the cycling of cross-links and possibly for some cellular energy transductions."}