A. Jorgensen

Publications46
h-index28
Citations3,056
Highly Influential Citations98
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Purification, Primary Structure, and Immunological Characterization of the 26-kDa Calsequestrin Binding Protein (Junctin) from Cardiac Junctional Sarcoplasmic Reticulum (*)
Previously we identified a protein of apparent M = 26,000 as the major calsequestrin binding protein in junctional sarcoplasmic reticulum vesicles isolated from cardiac and skeletal muscle (Mitchell,… Expand
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Structure and development of E-C coupling units in skeletal muscle.
Excitation-contraction (e-c) coupling depends on appropriate communication between the specialized, junctional domains of the sarcolemma/transverse tubules (jSUjT) and those of the sarcoplasmic… Expand
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Staining of the Ca2+-binding proteins, calsequestrin, calmodulin, troponin C, and S-100, with the cationic carbocyanine dye "Stains-all".
The Ca2+-binding proteins, calsequestrin, calmodulin, troponin C, and S-100, have all been shown to stain dark blue or purple with the cationic carbocyanine dye "Stains-all", while most proteins… Expand
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Purification and characterization of calsequestrin from canine cardiac sarcoplasmic reticulum and identification of the 53,000 dalton glycoprotein.
Cardiac calsequestrin was extracted from canine cardiac sarcoplasmic reticulum vesicles with Nonidet P-40 and purified by precipitation with calcium phosphate followed by fractionation on… Expand
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Biochemical Characterization and Molecular Cloning of Cardiac Triadin (*)
Triadin is an intrinsic membrane protein first identified in the skeletal muscle junctional sarcoplasmic reticulum and is considered to play an important role in excitation-contraction coupling.… Expand
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Dystrophin-glycoprotein complex and laminin colocalize to the sarcolemma and transverse tubules of cardiac muscle.
The expression and subcellular distribution of the dystrophin-glycoprotein complex and laminin were examined in cardiac muscle by immunoblot and immunofluorescence analysis of rabbit and sheep… Expand
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Biochemical characterization of ultrastructural localization of a major junctional sarcoplasmic reticulum glycoprotein (triadin).
Monoclonal antibodies were used to identify a 94-kDa protein that was greatly enriched in traids and junctional face membranes (9.3 +/- 0.2%) but not detected in the transverse tubular and… Expand
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Biogenesis of transverse tubules and triads: immunolocalization of the 1,4-dihydropyridine receptor, TS28, and the ryanodine receptor in rabbit skeletal muscle developing in situ
Our previous immunofluorescence studies support the conclusion that the temporal appearance and subcellular distribution of TS28 (a marker of transverse (T) tubules and caveolae in adult skeletal… Expand
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A monoclonal antibody to the Ca2+-ATPase of cardiac sarcoplasmic reticulum cross-reacts with slow type I but not with fast type II canine skeletal muscle fibers: an immunocytochemical and…
Ca2+-ATPase of the sarcoplasmic reticulum was localized in cryostat sections from three different adult canine skeletal muscles (gracilis, extensor carpi radialis, and superficial digitalis flexor)… Expand
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Two Structurally Distinct Calcium Storage Sites in Rat Cardiac Sarcopiasmic Reticulum: An Electron Microprobe Analysis Study
The elemental composition of subcellular organelles in resting rat papillary muscle was measured by electron probe x-ray microanalysis of cryosections of flash-frozen tissue. Nonmitochondrial… Expand
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