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B W Bell

Showing results (1-10 of 8) with videos related to

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Optics Letters|September 2, 2009
Moiré topography, sampling theory, and charged-coupled devicesB W Bell, C L Koliopoulos
Applied Optics|April 8, 2010
Single fiber light scattering matrix: an experimental determinationB W Bell, W S Bickel
The Journal of Biological Chemistry|February 15, 1988
The microheterogeneity of androgen-binding protein in rat serum and epididymis is due to differences in glycosylation of their subunitsB J Danzo, B W Bell
Biology of Reproduction|November 1, 1989
The microheterogeneity of rabbit testosterone-binding globulin is due to differential glycosylation of its single protomerB J Danzo, J H Black, B W Bell
Endocrinology|June 1, 1989
Human testosterone-binding globulin is a dimer composed of two identical protomers that are differentially glycosylatedB J Danzo, B W Bell, J H Black
Journal of Steroid Biochemistry|October 1, 1987
The apparent molecular weight of androgen-binding protein (ABP) in the blood of immature rats differs from that of ABP in the epididymisB J Danzo, B C Eller, B W Bell
The Journal of Steroid Biochemistry and Molecular Biology|January 1, 1991
Analysis of the oligosaccharides on androgen-binding proteins: implications concerning their role in structure/function relationshipsB J Danzo, J H Black, B W Bell
Endocrinology|June 1, 1988
Monoclonal antibodies to rat androgen-binding protein recognize both of its subunits and cross-react with rabbit and human testosterone-binding globulinW J Kovacs, B W Bell, M K Turney, et al.
Pageof 1

Showing results (1-10 of 8) with videos related to

Sort By:
Pageof 1
Optics Letters|September 2, 2009
Moiré topography, sampling theory, and charged-coupled devicesB W Bell, C L Koliopoulos
Applied Optics|April 8, 2010
Single fiber light scattering matrix: an experimental determinationB W Bell, W S Bickel
The Journal of Biological Chemistry|February 15, 1988
The microheterogeneity of androgen-binding protein in rat serum and epididymis is due to differences in glycosylation of their subunitsB J Danzo, B W Bell
Biology of Reproduction|November 1, 1989
The microheterogeneity of rabbit testosterone-binding globulin is due to differential glycosylation of its single protomerB J Danzo, J H Black, B W Bell
Endocrinology|June 1, 1989
Human testosterone-binding globulin is a dimer composed of two identical protomers that are differentially glycosylatedB J Danzo, B W Bell, J H Black
Journal of Steroid Biochemistry|October 1, 1987
The apparent molecular weight of androgen-binding protein (ABP) in the blood of immature rats differs from that of ABP in the epididymisB J Danzo, B C Eller, B W Bell
The Journal of Steroid Biochemistry and Molecular Biology|January 1, 1991
Analysis of the oligosaccharides on androgen-binding proteins: implications concerning their role in structure/function relationshipsB J Danzo, J H Black, B W Bell
Endocrinology|June 1, 1988
Monoclonal antibodies to rat androgen-binding protein recognize both of its subunits and cross-react with rabbit and human testosterone-binding globulinW J Kovacs, B W Bell, M K Turney, et al.
Pageof 1