PubMed HealthSearch

PubMed · 7213696

Human spectrin. VI. A viscometric study.

Abstract

Employing viscometry, human spectrin heterodimers and heterotetramers were analyzed in aqueous solution containing different amounts of salt. (1) In aqueous 0.1 M NaCl, pH 7.5, at 4 degrees C, the intrinsic viscosity of isolated human spectrin heterodimers and heterotetramers was found to be 40 +/- 6 and 79 +/- 7 ml/g, respectively. (2) The intrinsic viscosity of isolated human spectrin heterodimers and heterotetramers increased to 78 +/- 8 and 180 +/- 10 ml/g, respectively, as the ionic strength of the solution was reduced to about 2 mM. (3) This viscometric study indicates that isolated human spectrin heterodimers and heterotetramers are flexible molecules with a contour length of at least 110 and 200 nm, respectively.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

B T Stokke, A Elgsaeter. 1981-02-06. Human spectrin. VI. A viscometric study.. https://doi.org/10.1016/0005-2736(81)90094-8

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Production of waxy (amylose-free) wheats.

The Waxy (Wx) protein has been identified as granule-bound starch synthase (GBSS; EC 24.1.21), which is involved in amylose synthesis in plants. Although common wheat (Triticum aestivum L.) has three Wx proteins, "partial waxy mutants" lacking one or two of the three proteins have been found. Using such partial waxy mutants, tetra- and hexaploid waxy mutants with endosperms that are stained red-brown by iodine were produced. Both mutants showed loss of Wx protein and amylose. This is the first demonstration of genetic modification of wheat starch.

Electrophoresis, Polyacrylamide Gel

Measurement of protein in natural rubber latex.

Latex from the Brazilian rubber tree (Hevea brasiliensis) is the source of virtually all commercial natural rubber (cis-1,4-polyisoprene). Products made from natural rubber latex include gloves, condoms, and hundreds of different medical devices. However, recent reports of widespread life-threatening latex-associated Type I allergies have focused attention on latex proteins as serious allergens. In this paper, we describe a method that permits accurate and reproducible determination of protein in latex and that includes a procedure for solubilizing latex proteins and removing rubber. Also, we show that interfering substances in latex can be removed by precipitating proteins with sodium deoxycholate and trichloroacetic acid, and that latex proteins can be recovered and quantified with 2,2'-bicinchoninic acid.

Electrophoresis, Polyacrylamide Gel