scholarly journals Identification of gluten-like proteins in selected pod bearing leguminous tree seeds

PLoS ONE ◽  
2021 ◽  
Vol 16 (4) ◽  
pp. e0249427
Author(s):  
Mostafa Taghvaei ◽  
Brennan Smith ◽  
Gamze Yazar ◽  
Scott Bean ◽  
Michael Tilley ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Wheat Gluten ◽  
Seed Proteins ◽  
Protein Composition ◽  
Biochemical Properties ◽  
Coffee Tree ◽  
Vital Wheat Gluten ◽  
Tree Seeds ◽  
Coffee Seed

The protein composition, molecular weight distribution, and rheological properties of honey locust, mesquite, Kentucky coffee tree, and carob seed germs were compared against wheat gluten. Polymeric and Osborne fractionation protocols were used to assess biochemical properties. Dynamic oscillatory shear tests were performed to evaluate protein functionality. All samples had similar ratios of protein fractions as well as high molecular weight disulfide linked proteins except for the Kentucky coffee tree germ proteins, which were found to have lower molecular weight proteins with little disulfide polymerization. Samples were rich in acidic and polar amino acids (glutamic acid and arginine,). Rheological analyses showed that vital wheat gluten had the most stable network, while Kentucky coffee seed proteins had the weakest. High molecular weight disulfide linked glutenous proteins are a common, but not universal feature of pod bearing leguminous trees.

Heterogeneity of High-molecular-weight Human Salivary Mucins

2000 ◽  
Vol 14 (1) ◽  
pp. 69-75 ◽  
Author(s):  
G.D. Offner ◽  
R.F. Troxler
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Biochemical Properties ◽  
Salivary Proteins ◽  
Molecular Weights ◽  
Structural Framework ◽  
Buccal Epithelial Cells ◽  
Membrane Bound ◽  
Membrane Spanning ◽  
Micro Organisms

The existence of high-molecular-weight glycoproteins in saliva and salivary secretions has been recognized for nearly 30 years. These proteins, called mucins, are essential for oral health and perform many diverse functions in the oral cavity. Mucins have been intensively studied, and much has been learned about their biochemical properties and their interactions with oral micro-organisms and other salivary proteins. In the past several years, the major high-molecular-weight mucin in salivary secretions has been identified as MUC5B, one of a family of 11 human mucin gene products expressed in tissue-specific patterns in the gastrointestinal, respiratory, and reproductive tracts. MUC5B is one of four gel-forming mucins which exist as multimeric proteins with molecular weights greater than 20-40 million daltons. The heavily glycosylated mucin multimers form viscous layers which protect underlying epithelial surfaces from microbial, mechanical, and chemical assault. Another class of mucin molecules, the membrane-bound mucins, is structurally and functionally distinct from the gel-forming mucins. These proteins do not form multimers and can exist as both secreted and membrane-bound forms, with the latter anchored to epithelial cell membranes through a short membrane-spanning domain. In the present work, we show that two of the membrane-bound mucins, MUC1 and MUC4, are expressed in all major human salivary glands as well as in buccal epithelial cells. While the functions of these mucins in the oral environment are not understood, it is possible that they form a structural framework on the cell surface which not only is cytoprotective, but also may serve as a scaffold upon which MUC5B, and possibly other salivary proteins, assemble.

High molecular weight polypeptides related to dynein heavy chains in Nicotiana tabacum pollen tubes

1995 ◽  
Vol 108 (3) ◽  
pp. 1117-1125
Author(s):  
A. Moscatelli ◽  
C. Del Casino ◽  
L. Lozzi ◽  
G. Cai ◽  
M. Scali ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Nicotiana Tabacum ◽  
Pollen Tube ◽  
High Molecular Weight ◽  
Pollen Tubes ◽  
Biochemical Properties ◽  
Bovine Brain ◽  
Atp Binding ◽  
Heavy Chains ◽  
Dynein Heavy Chains

Nicotiana tabacum pollen tubes contain two high molecular weight polypeptides (about 400 kDa), which are specifically expressed during pollen germination and pollen tube growth in BK medium. The high molecular weight doublet resembles the dynein heavy chains in some biochemical properties. Sedimentation profiles of pollen tube extracts show that the high molecular weight bands have sedimentation coefficients of 22 S and 12 S, respectively. ATPase assay of sedimentation fractions shows an activity ten times higher when stimulated by the presence of bovine brain microtubules in fractions containing the 22 S high molecular weight polypeptide. Both these high molecular weight polypeptides can bind microtubules in an ATP-dependent fashion. A mouse antiserum to a synthetic peptide reproducing the sequence of the most conserved ATP-binding site among dynein heavy chains recognized the two high molecular weight polypeptides. Therefore these polypeptides have sequences immunologically related to the ATP binding sites of dynein heavy chains.

scholarly journals Wheat Gluten: High Molecular Weight Glutenin Subunits?Structure, Genetics, and Relation to Dough Elasticity

2007 ◽  
Vol 72 (3) ◽  
pp. R56-R63 ◽  
Author(s):  
Faqir Muhammad Anjum ◽  
Moazzam Rafiq Khan ◽  
Ahmad Din ◽  
Muhammad Saeed ◽  
Imran Pasha ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Wheat Gluten ◽  
Glutenin Subunits

Biochemical properties of some high molecular weight subunits of wheat glutenin

1985 ◽  
Vol 3 (1) ◽  
pp. 17-27 ◽  
Author(s):  
Johannes H.E. Moonen ◽  
Auke Scheepstra ◽  
Aris Graveland
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Biochemical Properties

Evaluation of baking properties and gluten protein composition of field grown transgenic wheat lines expressing high molecular weight glutenin gene 1Ax1

2001 ◽  
Vol 158 (4) ◽  
pp. 521-528 ◽  
Author(s):  
Indra K. Vasil ◽  
Scott Bean ◽  
Jianmin Zhao ◽  
Patrick McCluskey ◽  
George Lookhart ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Protein Composition ◽  
Transgenic Wheat ◽  
Gluten Protein ◽  
Wheat Lines

Variation and inheritance of cytosine methylation patterns in wheat at the high molecular weight glutenin and ribosomal RNA gene loci

Development ◽  
1990 ◽  
Vol 108 (Supplement) ◽  
pp. 15-20
Author(s):  
R. B. Flavell ◽  
M. O'Dell
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Cytosine Methylation ◽  
Seed Proteins ◽  
New Variant ◽  
Hmw Glutenin ◽  
Transcription Complexes ◽  
Methylation Patterns ◽  
Sexual Crosses ◽  
Rna Genes

Chromosome marking by cytosine methyiation has been examined in two gene systems in wheat – at the loci encoding high molecular weight (HMW) glutenin subunits (seed proteins) and ribosomai RNA. Variation in cytosine methyiation occurs between progeny in highly inbred lines around the HMW glutenin locus. The variation is inherited through meiosis to F1, and F2 generations but occasionally a new variant arises. Specific cytosine residues lose their methyl group in the seed, the organ where the genes are expressed. Within the multigene family of ribosomai RNA genes, several subsets of genes can be defined based upon the cytosine methylation patterns. High activity of a ribosomai RNA gene locus is correlated with loss of methylation at specific cytosine residues, especially in the promoter and upstream regulatory regions. A model is described in which the subset of genes selected to be used are those to which specific regulatory proteins and transcription complexes bind most favourably. Binding of such proteins inhibits cytosine methylation and so marks the subset of genes for expression in subsequent cell generations. Examples are described where new types of RNA genes are introduced via sexual crosses that result in changes to the methylation patterns of the ribosomai RNA genes. The processes determining the changes begin, it is believed, in the fertilised egg.

scholarly journals Subaxolemmal cytoskeleton in squid giant axon. I. Biochemical analysis of microtubules, microfilaments, and their associated high-molecular-weight proteins.

1986 ◽  
Vol 102 (5) ◽  
pp. 1699-1709 ◽  
Author(s):  
T Kobayashi ◽  
S Tsukita ◽  
S Tsukita ◽  
Y Yamamoto ◽  
G Matsumoto
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Actin Filaments ◽  
Giant Axon ◽  
Protein Molecule ◽  
Biochemical Properties ◽  
Cross Reactivity ◽  
Squid Giant Axon ◽  
Molecular Organization ◽  
Nacl Solution

Using the squid giant axon, we analyzed biochemically the molecular organization of the axonal cytoskeleton underlying the axolemma (subaxolemmal cytoskeleton). The preparation enriched in the subaxolemmal cytoskeleton was obtained by squeezing out the central part of the axoplasm using a roller. The electrophoretic banding pattern of the subaxolemmal cytoskeleton was characterized by large amounts of two high-molecular-weight (HMW) proteins (260 and 255 kD). The alpha, beta-tubulin, actin, and some other proteins were also its major constituents. The 260-kD protein is known to play an important role in maintaining the excitability of the axolemma (Matsumoto, G., M. Ichikawa, A. Tasaki, H. Murofushi, and H. Sakai, 1983, J. Membr. Biol., 77:77-91) and was recently designated "axolinin" (Sakai, H., G. Matsumoto, and H. Murofushi, 1985, Adv. Biophys., 19:43-89). We purified axolinin and the 255-kD protein in their native forms and further characterized their biochemical properties. The purified axolinin was soluble in 0.6 M NaCl solution but insoluble in 0.1 M NaCl solution. It co-sedimented with microtubules but not with actin filaments. In low-angle rotary-shadowing electron microscopy, the axolinin molecule in 0.6 M NaCl solution looked like a straight rod approximately 105 nm in length with a globular head at one end. On the other hand, the purified 255-kD protein was soluble in both 0.1 and 0.6 M NaCl solution and co-sedimented with actin filaments but not with microtubules. The 255-kD protein molecule appeared as a characteristic horseshoe-shaped structure approximately 35 nm in diameter. Furthermore, the 255-kD protein showed no cross-reactivity to the anti-axolinin antibody. Taken together, these characteristics lead us to conclude that the subaxolemmal cytoskeleton in the squid giant axon is highly specialized, and is mainly composed of microtubules and a microtubule-associated HMW protein (axolinin), and actin filaments and an actin filament-associated HMW protein (255-kD protein).

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