نتایج جستجو برای: 34 kd protein

تعداد نتایج: 1345417  

Journal: :The Journal of Cell Biology 1993
P B Scotland M Colledge I Melnikova Z Dai S C Froehner

A postsynaptic membrane-associated protein of M(r) 43,000 (43-kD protein) is involved in clustering of the nicotinic acetylcholine receptor (AChR) at the neuromuscular junction. Previous studies have shown that recombinant mouse 43-kD protein forms membrane-associated clusters when expressed in Xenopus oocytes. Coexpression with the AChR results in colocalization of the receptor with the 43-kD ...

Journal: :Blood 1993
R D Baynes G K Reddy Y J Shih B S Skikne J D Cook

The present investigation was undertaken to search for soluble forms of the erythropoietin receptor in human serum using polyclonal antibody against an amino terminal peptide sequence in the extracellular domain. This sequence was located adjacent to the amino terminus at residues 25-38. When this antibody was used for Western blots of solubilized membranes from nucleated bone marrow cells, a p...

Journal: :Plant physiology 2001
K Yamada R Matsushima M Nishimura I Hara-Nishimura

Arabidopsis RD21 is a cysteine protease of the papain family. Unlike other members of the papain family, RD21 has a C-terminal extension sequence composed of two domains, a 2-kD proline-rich domain and a 10-kD domain homologous to animal epithelin/granulin family proteins. The RD21 protein was accumulated as 38- and 33-kD proteins in Arabidopsis leaves. An immunoblot showed that the 38-kD prote...

Journal: :Biochemical Journal 2021

Metal ions play many critical roles in biology, as structural and catalytic cofactors, cell regulatory signalling elements. The metal–protein affinity, expressed conveniently by the metal dissociation constant, KD, describes thermodynamic strength of a interaction is key parameter that can be used, for example, to understand how proteins may acquire metals identify dynamic elements (e.g. cofact...

Journal: :Plant physiology 2001
W Werhahn A Niemeyer L Jänsch V Kruft U K Schmitz H Braun

The translocase of the outer mitochondrial membrane (TOM) complex is a preprotein translocase that mediates transport of nuclear-encoded mitochondrial proteins across the outer mitochondrial membrane. Here we report the purification of this protein complex from Arabidopsis. On blue-native gels the Arabidopsis TOM complex runs at 230 kD and can be dissected into subunits of 34, 23, 21, 8, 7, and...

Journal: :Domestic animal endocrinology 2007
Thomas J Caperna Amy E Shannon Mark P Richards Wesley M Garrett Neil C Talbot

Aquaporins (AQPs) are members of a large family of integral membrane proteins involved in the rapid movement of water and neutral solutes across cell membranes. In this study, we have prepared an affinity-purified porcine-specific polyclonal antiserum to AQP9 and have investigated the distribution and expression of AQP9 in pig liver tissue and in hepatocytes in primary culture. Immunocytochemic...

Journal: :Investigative ophthalmology & visual science 1990
O P Srivastava K Srivastava S D Shukla

The pellet recovered after centrifugation (5000 X g) of human corneal endothelial homogenates was used as the source of membranes in these studies. A 66-kilodalton (kD) protein was identified as the most abundant protein in the particulate pellet by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis. The de novo synthesis of the 66-kD protein by endothelial cells was observed durin...

Journal: :The Journal of Experimental Medicine 1988
J D Haynes J P Dalton F W Klotz M H McGinniss T J Hadley D E Hudson L H Miller

A 135-kD parasite protein, a minor component of the Plasmodium knowlesi malaria radiolabeled proteins released into culture supernatant at the time of merozoite release and reinvasion, specifically bound to human erythrocytes that are invaded and carry a Duffy blood group determinant (Fya or Fyb), but did not bind to human erythrocytes that are not invaded and do not carry a Duffy determinant (...

Journal: :The Journal of Cell Biology 1992
J A Johnston R D Sloboda

A protein of 62 kD is a substrate of a calcium/calmodulin-dependent protein kinase, and both proteins copurify with isolated mitotic apparatuses (Dinsmore, J. H., and R. D. Sloboda. 1988. Cell. 53:769-780). Phosphorylation of the 62-kD protein increases after fertilization; maximum incorporation of phosphate occurs during late metaphase and anaphase and correlates directly with microtubule disa...

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