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B L Horecker

Showing results (141-150 of 182) with videos related to

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Proceedings of the National Academy of Sciences of the United States of America|January 1, 1981
Purification of thymus mRNA coding for a 16,000-dalton polypeptide containing the thymosin alpha 1 sequenceM Freire, E Hannappel, M Rey, et al.
Archives of Biochemistry and Biophysics|October 1, 1974
Transformation of neutral to alkaline fructose 1,6-bisphosphatase. Converting enzyme activity in the large-particle fraction from rabbit liverS Pontremoli, A Accorsi, E Melloni, et al.
Biochemical and Biophysical Research Communications|September 9, 1974
Evidence for the modification of fructose 1,6-bisphosphatase by two distinct lysosomal proteasesS Pontremoli, E Melloni, A Accorsi, et al.
Archives of Biochemistry and Biophysics|August 1, 1991
Identification of two calpastatin forms in rat skeletal muscle and their susceptibility to digestion by homologous calpainsS Pontremoli, E Melloni, P L Viotti, et al.
Proceedings of the National Academy of Sciences of the United States of America|January 1, 1987
Phosphorylation by protein kinase C of a 20-kDa cytoskeletal polypeptide enhances its susceptibility to digestion by calpainS Pontremoli, E Melloni, M Michetti, et al.
Proceedings of the National Academy of Sciences of the United States of America|December 1, 1973
Changes in rabbit-liver lysosomes and fructose 1,6-bisphosphatase induced by cold and fastingS Pontremoli, E Melloni, F Salamino, et al.
Biochemical and Biophysical Research Communications|June 14, 1985
Role of phospholipids in the activation of the Ca2+-dependent neutral proteinase of human erythrocytesS Pontremoli, E Melloni, B Sparatore, et al.
Biochemical and Biophysical Research Communications|April 16, 1985
Binding to erythrocyte membrane is the physiological mechanism for activation of Ca2+-dependent neutral proteinaseS Pontremoli, E Melloni, B Sparatore, et al.
Methods in Enzymology|January 1, 1982
Fructose-1,6-bisphosphatase from chicken and rabbit muscleJ S MacGregor, A E Annamalai, A van Tol, et al.
The Journal of Biological Chemistry|February 5, 1988
Effects of a monoclonal anti-calpain antibody on responses of stimulated human neutrophils. Evidence for a role for proteolytically modified protein kinase CS Pontremoli, E Melloni, G Damiani, et al.
Pageof 19

Showing results (141-150 of 182) with videos related to

Sort By:
Pageof 19
Proceedings of the National Academy of Sciences of the United States of America|January 1, 1981
Purification of thymus mRNA coding for a 16,000-dalton polypeptide containing the thymosin alpha 1 sequenceM Freire, E Hannappel, M Rey, et al.
Archives of Biochemistry and Biophysics|October 1, 1974
Transformation of neutral to alkaline fructose 1,6-bisphosphatase. Converting enzyme activity in the large-particle fraction from rabbit liverS Pontremoli, A Accorsi, E Melloni, et al.
Biochemical and Biophysical Research Communications|September 9, 1974
Evidence for the modification of fructose 1,6-bisphosphatase by two distinct lysosomal proteasesS Pontremoli, E Melloni, A Accorsi, et al.
Archives of Biochemistry and Biophysics|August 1, 1991
Identification of two calpastatin forms in rat skeletal muscle and their susceptibility to digestion by homologous calpainsS Pontremoli, E Melloni, P L Viotti, et al.
Proceedings of the National Academy of Sciences of the United States of America|January 1, 1987
Phosphorylation by protein kinase C of a 20-kDa cytoskeletal polypeptide enhances its susceptibility to digestion by calpainS Pontremoli, E Melloni, M Michetti, et al.
Proceedings of the National Academy of Sciences of the United States of America|December 1, 1973
Changes in rabbit-liver lysosomes and fructose 1,6-bisphosphatase induced by cold and fastingS Pontremoli, E Melloni, F Salamino, et al.
Biochemical and Biophysical Research Communications|June 14, 1985
Role of phospholipids in the activation of the Ca2+-dependent neutral proteinase of human erythrocytesS Pontremoli, E Melloni, B Sparatore, et al.
Biochemical and Biophysical Research Communications|April 16, 1985
Binding to erythrocyte membrane is the physiological mechanism for activation of Ca2+-dependent neutral proteinaseS Pontremoli, E Melloni, B Sparatore, et al.
Methods in Enzymology|January 1, 1982
Fructose-1,6-bisphosphatase from chicken and rabbit muscleJ S MacGregor, A E Annamalai, A van Tol, et al.
The Journal of Biological Chemistry|February 5, 1988
Effects of a monoclonal anti-calpain antibody on responses of stimulated human neutrophils. Evidence for a role for proteolytically modified protein kinase CS Pontremoli, E Melloni, G Damiani, et al.
Pageof 19