Number Of Chains Research Articles

The construction of fuzzy subgroups of groups with units modulo 20 and 21

The number of fuzzy subgroups (NFSGs) of the groups of units U20 and U21 are determining in this study. The (NFSGs) of U20 was found based on diagram and using the lemma which state that the (NFSGs) of G is equal to the number of chains (NC) on the subgroups lattice of G. Moreover, we explain that there are only two fuzzy subgroups for a prime order group. Lagrange’s theorem is more important in this work, from Lagrange’s theorem, there is no nontrivial subgroup of U21 since the order of the group is prime. We prove that, if P1 (μ) = U21, then we get μ1(x) = θ1, ∀x ∈ U21. Thus we have one fuzzy subgroup of P1 (μ) = U21. If P1 (μ) = {1}, then we obtain μ2(x) = θ1, ∀x ∈ {1} and μ2 (x) = θ2,∀x∈U21\{1}. Thus we have 2 fuzzy subgroups of U21. We came up with the numbers 21 and 2 respectively.

Impact of full range of amylose contents on the architecture of starch granules*

The effects of amylose deposition on crystalline regions of barley starch granules were studied in granules containing zero to 99.1% amylose using “waxy” (WBS, 0% amylose), normal (NBS, 18% amylose) and amylose-only barley lines (AOS, 99.1% amylose). The effects were probed after hydrolysis of amorphous regions of starch granules in dilute HCl generating lintners, which typically represent the crystalline lamella of starch granules. Compared to NBS and WBS, AOS granules exhibited an irregular, multilobular morphology with a rough surface texture. AOS displayed lower rates of acid hydrolysis than WBS, and AOS reached a plateau at ∼45wt% acid hydrolysis. High-performance anion-exchange chromatography of lintners at equivalent levels of hydrolysis (45wt%) revealed the average degree of polymerization (DP) of AOS lintners was 21, substantially smaller than that of NBS and WBS (DP 42). AOS lintners contained the lowest number of chains (NC) per molecule (1.1) compared to NBS (2.8) and WBS (3.3) and the average chain length of AOS, NBS and WBS lintners was 19, 15 and 13, respectively. Hence, both NC and the average chain length correlated with amylose content. The size distribution profile of AOS lintners revealed a repeat motif in the molecules corresponding to 5–6 glucose residues.

Chemical compositions, fine structure and physicochemical properties of kudzu ( Pueraria lobata) starches from different regions

Three commercial kudzu starches from Vietnam, Japan and Korea were used to determine chemical compositions, isoflavone compounds, fine structure and physicochemical properties. The kudzu starch from Vietnam had polygonal granules, whereas the kudzu starches from Japan and Korea contained both polygonal and spherical granules. Total protein, lipid, ash and phosphorus contents present in these kudzu starches were less than 1% (starch basis). The kudzu starch from Vietnam and Korea contained both daidzein and daidzin, whereas the kudzu starch from Japan had only daidzein. These starches had similar actual amylose contents (22.2–22.9%). However, λ max, blue value and apparent amylose contents of the kudzu starch from Vietnam were lower than those from Japan and Korea. Amylose molecules of the kudzu starch from Vietnam had the largest average degree of polymerization (DP n ) and number of chains (NC), followed by the kudzu starches from Japan and Korea. Amylopectin molecules of the kudzu starch from Vietnam also had the largest DP n and NC, followed by the kudzu starches from Korea and Japan. X-ray diffraction patterns of the kudzu starches from Vietnam, Japan and Korea were A-type, C-type and B-type, respectively. The kudzu starch from Vietnam was found to have the specific characteristics such as significantly high gelatinization temperature, transition enthalpy and degree of crystallinity as compared to the kudzu starch from Korea and Japan.

Rheological properties of rice amylose gels and their relationships to the structures of amylose and its subfractions

Rice amyloses, extracted from three rice starches (KSS7, TCS10 and TNu67), were used in this study. The rheological properties of amylose gels (3%, w/w) and the structures of amylose and its subfractions were investigated, the relationships between rheological properties and structures of amylose were then considered. During aging for 5 h, TCS10 amylose gel showed the greatest G initial ′ and G final ′ values and the lowest tan δ initial and tan δ final values among the three amylose gels studied. On the other hand, TNu67 amylose gel had the lowest G initial ′ and G final ′ values. The DP n (number-average degree of polymerization) of rice amyloses studied ranged from 1004 to 1289. The GPC profiles of the amyloses, on a TSK HW-65F column, showed bimodal distributions and the amyloses could be separated into subfractions with larger ( F1) and smaller ( F2) molecular weights. Among the samples studied, TCS10 had the greatest DP n and longest CL (average chain length) for amylose and the F1 and F2 subfractions. KSS7 and TNu67 had similar DP n for the amylose and subfractions, while the CL of the F1 and F2 amylose subfractions of KSS7 were longer than those of TNu67. The subfractions of TNu67 amylose also showed obviously greater NC (number of chains per molecule) and lower β-amylolysis limit than did the other amyloses studied. Results indicated that the rheological properties of rice amylose gel were highly related to the structures of amylose and its subfractions. Amylose with greater DP n , longer CL, and smaller NC led to an amylose gel with higher gel strength or elasticity.

The possible role of glycoproteins in neural function.

BRIEF PROPOSALS THE POSSIBLE ROLE OF GLYCOPROTEINS IN NEURAL FUNCTION ERIC G. BRUNNGRABER, Ph.D.* The structural complexity ofa protein is determined by die sequence ofamino acids in the peptide chains of which it is composed and by the geometrical arrangement of these chains in three-dimensional space. Glycoproteins characteristically contain carbohydrate chains; these are attached at various points along die polypeptide chains. The inherent complexity of the carbohydrate portion of the glycoprotein molecule causes a manifold increase ofthe complexity ofdie totalstructure. The sugars that commonlyform a part ofdiese polysaccharide chains include N-acetylneuraminic acid, fucose, galactose, mannose, glucosamine, and galactosamine. It is possible to have a linearsequence ofsugars that form repeating units consisting ofhexosamine and hexose. It is also possible to have highly branched polysaccharides. Furthermore, the chains may be quite small or as large as a small proteinmolecule. N-acetylneuraminic acid and fucose, ifpresent, are invariably glycosidically linked as terminal groups. These two sugars possess unique properties. Fucose contains a mediyl group, endowing die molecule widi a lipophilic group not present inothersugars. N-acetylneuraminic acid contains acarboxyl group, endowing die molecule with a negative charge. The possible variations in the structure of the polysaccharide chains seem almost infinite, aldiough future research will doubtless provide some measure oforder in the number ofchain types that nature has devised. Brain tissue contains a minimum of nine chain types diat differ in molecular size, charge, and sugar composition. Future separation methods will undoubtedly uncover a much larger number ofchain types. A single glycoprotein molecule may contain more than one polysaccharide chain, and die number and chemical characteristics ofthe many polysaccharide chains attached to die protein molecule allow for many possible macromolecular structures. The inherent polymorphism of the glycoprotein molecule—the many possible permutations and combinations in the location, chemical structure, and configuration ofthe polysaccharide side chains—suggests that the glycoprotein molecule is a reasonable candidate for future investigations designed to elucidate macromolecular alterations due to functional activity in the central nervous system. Brain tissue contains a high concentration ofglycoproteins. It can be calculated that as much as 5-15 per cent ofdie total protein content ofthis tissue may consist ofglycoprotein . But much more important is the finding that most ofthese glycoproteins are mem- * Illinois State Psychiatric Institute, 1601 West Taylor Street, Chicago, Illinois 60612. 467 brane bound. Strenuous homogenization of die tissue widi the purpose of obtaining glycoproteins in soluble form can extract only 20-30 per cent ofdie total glycoprotein of brain tissue. The rest remains bound to die lipid-rich residue. Analysis ofnerve endings, axonal fragments, and other membranous structures, obtained by density-gradient centrifugation of brain tissue diat had been homogenized under controlled conditions, has revealed the close association ofglycoproteins with such structures. The synaptic region, through which impulses must pass in order to continue dieirjourney from cell to neighboring cell, contains a high concentration ofmembrane-bound glycoproteins. So do die axons and the fragments diat are derived from other membranes ofthe neuron and glia cell. Glycoproteins are not conspicuous in the cytoplasm. The results ofsubcellular fractionation studies are readily reconcilable with the observations of histochemists, who uniformly find that carbohydrate-rich material fills the spaces between adjacent nerve cells and is especially concentrated in die synaptic regions. In general, glycoproteins are present in high concentration in extracellular fluids. Glycoproteins are also important structural components of die plasma membrane of a wide variety ofcell types. Apparently these substances are synthesized within die cell in ordertoperform an extracellular function. In some cases the secreted glycoprotein functions at locations remote from the site ofsyndiesis. In other cases the secreted glycoprotein appears to function at die cell surface or in die intercellular space immediately adjacent to the parent cell, thereby playing a role in the relationship of die cell and its immediate environment. Most secreted proteins are glycoproteins, while most intracellular proteins are not. It appears diat brain glycoproteins are not an exception. Although synthesized in the nerve cell body, probably in the Golgi region, diey migrate to the cell surface. During this migration, additional sugar residues may be added to die molecule. Secretion appears to be limited to a process in which the glycoprotein becomes deposited upon the outer portion ofdie...