Zobrazeno 1 - 10
of 29
pro vyhledávání: '"Andrew O. Martinez"'
Autor:
Roberto M. Aguilar, Juan J. Bustamante, Luis S. Haro, Alexei L. Grigorian, Andrew O. Martinez, Lisa R. Treviño, Jesus Muñoz
Publikováno v:
Growth Hormone & IGF Research. 20:298-304
Background Human growth hormone (hGH) is a complex mixture of molecular isoforms. Gaps in our knowledge exist regarding the structures and biological significances of the uncharacterized hGH molecular variants. Mercaptoethanol-resistant 45-kDa human
Autor:
Roberto M. Aguilar, Andrew O. Martinez, Jesus Muñoz, Lisa R. Treviño, Luis S. Haro, Juan J. Bustamante, Frank Talamantes
Publikováno v:
Journal of Peptide Science. 15:78-88
The membrane-bound rat GH-R and an alternatively spliced isoform, the soluble rat GH-BP, are comprised of identical N-terminal GH-binding domains; however, their C-terminal sequences differ. Immunological reagents are needed to distinguish between th
Autor:
Roberto M. Aguilar, Luis S. Haro, Alexei L. Grigorian, Jesus Muñoz, Andrew O. Martinez, Juan J. Bustamante
Publikováno v:
ELECTROPHORESIS. 28:3829-3836
The 40-60 pituitary human growth hormone (hGH) isoforms are so similar in their physico-chemical properties (charge, size, hydrophobicity) that the limited resolutions of chromatographic separation methodologies have not permitted most of them to be
2-D native-PAGE/SDS-PAGE visualization of an oligomer's subunits: Application to the analysis of IgG
Autor:
Andrew O. Martinez, Luis S. Haro, Edwin J. Barea-Rodriguez, Leticia Gonzalez, Juan J. Bustamante
Publikováno v:
ELECTROPHORESIS. 27:2016-2023
A 2-D native-PAGE/SDS-PAGE method for detecting the subunit components of protein oligomers at low picomole sensitivity is presented. IgG was electrophoresed in a native acidic polyacrylamide gel in amounts ranging from 51 pmol to 60 fmol. Silver-sta
Autor:
Roberto M. Aguilar, Andrew O. Martinez, Rafael Flores, Juan J. Bustamante, Ana Trevino, Luis S. Haro, Macario Garcia, Jesus A. Garcia, Luis Benavides, Leticia Gonzalez
Publikováno v:
ELECTROPHORESIS. 26:4389-4395
A method for separating proteins with a molecular mass difference of 2 kDa using SDS-PAGE under nonreducing conditions is presented. A sample mixture containing several human growth hormone (hGH) isoforms was initially separated on a weak anion-excha
Publikováno v:
Protein Science. 14:902-913
Although a 22-kDa human growth hormone (hGH) is the predicted protein product of the hGH-N gene, a pleiotropic collection of uncharacterized molecular weight and charge isoforms is also produced. Using chromatography and preparative SDS-PAGE under re
Autor:
Rafael Flores, C.C López-Guajardo, Roberto M. Aguilar, Juan J. Bustamante, Luis S. Haro, Andrew O. Martinez, P. Hernandez
Publikováno v:
Molecular and Cellular Endocrinology. 152:179-187
In this report we present the first in-depth description of the biochemical and pharmacological properties of rabbit cardiac GH receptors. The apparent M r ’s of the [ 125 I]human (h) GH-receptor complexes were 380, 205, 90, 62, 52 and 38 kDa as de
Publikováno v:
Analytical Biochemistry. 267:344-350
SDS–PAGE of chromatographic fractions requires prior removal of salts, detergents, denaturants, or organic solvents which may perturb the electrophoretic separation. Likewise, to successfully visualize minute amounts of protein present in chromatog
Publikováno v:
Analytical Biochemistry. 265:232-237
A technique for carbohydrate analysis that is both inexpensive and easily performed is currently unavailable. In this communication we address the problem and have outlined a method for labeling saccharides with a visible dye, 4-amino-1,1'-azobenzene
Publikováno v:
Journal of Chromatography B: Biomedical Sciences and Applications. 720:39-47
Human GH isoforms were separated by anion-exchange chromatography using a linear NaCl gradient in the presence and absence of EDTA and EGTA. SDS-PAGE showed that glycosylated 24-kDa hGH did not appreciably separate from other hGH variants in the abse