scholarly journals Enzymes of Aspergillus Oryzae V. Ethanol Fractionation at Low Ionic Strengths

1953 ◽  
Vol 6 (3) ◽  
pp. 447 ◽  
Author(s):  
JM Gillespie ◽  
EFW ood
Keyword(s):  
Aspergillus Oryzae ◽  
Moving Boundary ◽  
Paper Electrophoresis ◽  
Minor Components ◽  
Enzyme Preparations ◽  
Main Protein ◽  
Protein Components ◽  
Paper Method

Moving boundary and paper electrophoresis were applied to crude and deionized enzyme preparations from cultures of Aspergillus oryzae. Five main protein components were observed by both methods and four additional minor components were demonstrated with the paper method.

Studies of Casein. I. Some Observations on the Heterogeneity of Casein Fractions

1959 ◽  
Vol 12 (4) ◽  
pp. 712 ◽  
Author(s):  
HA McKenzie ◽  
RG Wake
Keyword(s):  
Filter Paper ◽  
Paper Electrophoresis ◽  
The Other ◽  
Minor Components ◽  
Casein Micelles ◽  
Protective Colloid ◽  
Alcohol Fraction ◽  
Minor Protein ◽  
Fractionation Method ◽  
Protein Components

The heterogeneity of casein is discussed in the light of methods currently used for the fractionation of casein. In particular, the possible heterogeneity of certain preparations of α-casein is considered. This is important because it has been generally considered that α-casein is the protective colloid which is altered when the enzyme, rennin, acts on casein micelles. Recently, Waugh and von Hippel (1956) have suggested that their new component x-casein, and not α-casein, is the protective colloid. These two viewpoints could be reconciled if α-casein samples previously examined contained x-casein as well. In the present work, a study is made of filter paper electrophoresis, micelle-forming properties, and sedimentation of casein fractions. It is shown that x-casein is concentrated with α-casein in fraction A during the alcohol fractionation method of Hipp et al. (1952). On the other hand fraction B contains α-casein essentially free of x-casein. The a-casein obtained in the urea fractionation method of Hipp et al. also contains x-casein. Thus only alcohol fraction B is a suitable source of pure α-casein. During the paper electrophoretic examination of casein fractions a number of minor protein components are observed. A component moving more slowly than γ-casein is present in acid casein, second-cycle casein-fraction P, and an alcohol fraction. This component was first observed in the latter fraction by Hipp et al. (1952) when preparing γ-casein. Electropherograms of second-cycle casein-fraction S indicate the presence of x-, β-, and γ-casein, and two minor components moving between x- and β The way in which these components arise is briefly discussed.

scholarly journals Oogenesis and egg development in triatomines: a biochemical approach

2005 ◽  
Vol 77 (3) ◽  
pp. 405-430 ◽  
Author(s):  
Georgia C. Atella ◽  
Katia C. Gondim ◽  
Ednildo A. Machado ◽  
Marcelo N. Medeiros ◽  
Mário A.C. Silva-Neto ◽  
...  
Keyword(s):  
Fat Body ◽  
Ovarian Tissue ◽  
Late Phase ◽  
Instar Nymph ◽  
Minor Components ◽  
Yolk Proteins ◽  
First Instar ◽  
Main Protein ◽  
Biochemical Approach ◽  
Protein Components

In triatomines, as well as in other insects, accumulation of yolk is a process in which an extra-ovarian tissue, the fat body, produces yolk proteins that are packed in the egg. The main protein, synthesized by the fat body, which is accumulated inside the oocyte, is vitellogenin. This process is also known as vitellogenesis. There are growing evidences in triatomines that besides fat body the ovary also produces yolk proteins. The way these yolk proteins enter the oocyte will be discussed. Yolk is a complex material composed of proteins, lipids, carbohydrates and other minor components which are packed inside the oocyte in an organized manner. Fertilization triggers embryogenesis, a process where an embryo will develop. During embryogenesis the yolk will be used for the construction of a new individual, the first instar nymph. The challenge for the next decade is to understand how and where these egg proteins are used up together with their non-protein components, in pace with the genetic program of the embryo, which enables cell differentiation (early phase of embryogenesis) and embryo differentiation (late phase) inside the egg.

Tactoid formation in deer hemoglobin

1960 ◽  
Vol 199 (1) ◽  
pp. 190-192 ◽  
Author(s):  
John H. Moon
Keyword(s):  
Odocoileus Virginianus ◽  
Sickle Cell ◽  
Moving Boundary ◽  
Paper Electrophoresis ◽  
Free Hemoglobin ◽  
Hemoglobin Solution ◽  
Hunting Season ◽  
Phase Microscopy ◽  
Veronal Buffer ◽  
Kinetics Of

Sickle cell preparations were made on eight Virginia white-tail deer ( Odocoileus virginianus) killed during the 1958–59 hunting season. All preparations showed sickling. Paper electrophoresis of carboxyhemoglobin from these animals revealed identical mobilities and a single hemoglobin component present at pH 8.6. Alkali denaturation of the deer carboxyhemoglobin solution showed that it was markedly resistant to alkali denaturation and that the kinetics of the denaturation were different from that of human cord hemoglobin. Deer carboxyhemoglobin migrated 0.6 x 10–5 cm2/volt/sec.–1 faster than human carboxyhemoglobin A in moving boundary electrophoresis in veronal buffer at pH 8.2. Tactoids were demonstrated in free hemoglobin solution with phase microscopy after concentration of the solution. These particles are very similar morphologically to these prepared from hemoglobin solution containing hemoglobin S.

Re-Investigation of the Protein Structure of Coenzyme B12-Dependent Diol Dehydrase

1987 ◽  
Vol 42 (4) ◽  
pp. 353-359 ◽  
Author(s):  
Katsuyuki Tanizawa ◽  
Nobuyoshi Nakajima ◽  
Tetsuo Toraya ◽  
Hidehiko Tanaka ◽  
Kenji Soda
Keyword(s):  
Protein Structure ◽  
Membrane Fraction ◽  
Enzyme Purification ◽  
Soluble Fraction ◽  
Proteolytic Cleavage ◽  
Subunit Structure ◽  
Coenzyme B12 ◽  
Enzyme Preparations ◽  
Protein Components ◽  
Limited Digestion

We have purified diol dehydrase, an adenosylcobalamin-dependent enzyme, from Klebsiella pneumoniae by two different procedures to re-investigate its protein structure; one including its extraction with detergent from the membrane fraction, and the other consisting of only chromato­graphic separations of the soluble fraction. The enzyme preparations obtained by these two methods were different in the subunit structure, but both are identical in molecular weight, and in enzymological and immunochemical properties. In addition, the enzyme preparation obtained from the membrane fraction dissociated reversibly into two dissimilar protein components (F and S) in the absence of substrate, as did the preparation from the soluble fraction. Although the subunit multiplicity of component S might be partly due to proteolytic cleavage during the enzyme purification as revealed by limited digestion with trypsin, component F is not a product of proteolytic cleavage of component S, but a primordial and essential constituent of the enzyme.

Quantitative Electrophoresis of Serum Proteins on Paper

1956 ◽  
Vol 2 (5) ◽  
pp. 303-319 ◽  
Author(s):  
Moses Wurm ◽  
Frederick H Epstein
Keyword(s):  
Protein Concentration ◽  
Moving Boundary ◽  
Serum Proteins ◽  
Paper Electrophoresis ◽  
Bromphenol Blue ◽  
Good Resolution ◽  
Confidence Limits ◽  
Protein Patterns ◽  
Electrophoretic Patterns ◽  
Normal Human

Abstract 1. A procedure for paper electrophoresis has been described which gives highly reproducible protein patterns with good resolution and freedom from distortions. 2. Densitometry of protein bands on paper stained with bromphenol blue or Amidoschwarz 10B reveals that the logarithm of protein concentration is proportional to optical density and that Beer's law does not apply. Electrophoretic patterns of normal human serum evaluated in this manner give values in close agreement with those obtained by moving-boundary electrophoresis. 3. Confidence limits were determined for both methods.

Differential polymerization of the two main protein components of dragline silk during fibre spinning

2005 ◽  
Vol 4 (10) ◽  
pp. 772-775 ◽  
Author(s):  
Alexander Sponner ◽  
Eberhard Unger ◽  
Frank Grosse ◽  
Klaus Weisshart
Keyword(s):  
Dragline Silk ◽  
Fibre Spinning ◽  
Main Protein ◽  
Protein Components

Taxonomic significance of seed protein profiles in Acacia, with special reference to Acacia emilioana

2003 ◽  
Vol 16 (1) ◽  
pp. 35 ◽  
Author(s):  
Alicia L. Lamarque ◽  
Renée H. Fortunato
Keyword(s):  
Seed Protein ◽  
Seed Proteins ◽  
High Concentration ◽  
Protein Patterns ◽  
Qualitative And Quantitative ◽  
Sds Page ◽  
Electrophoretic Data ◽  
Main Protein ◽  
Protein Components ◽  
Total Seed

Total seed proteins of 10 Acacia species were examined by SDS–PAGE. The protein patterns showed qualitative and quantitative differences among the taxa analysed. The main protein components of most species examined had MW's in the range of 38.5–49.0 × 103. Subgenus Aculeiferum differed from subg. Acacia in the presence of a high concentration of proteins in the range of 20–24.5 × 103. Hierarchical clustering of the 10 taxa was undertaken, based on Jaccard distances calculated from electrophoretic data. The species grouped in two main clusters, representing the two subgenera of Acacia that occur in America, namely subg. Acacia and subg. Aculeiferum. The taxonomic placement of Acacia emilioana, a species with uncertain sectional affinity within subg. Aculeiferum, is discussed.

scholarly journals HYDROLYTIC REGULATION OF COMPONENT PROPERTIES

2020 ◽  
Vol 6 (444) ◽  
pp. 23-28
Author(s):  
V. A. Asafov ◽  
◽  
N. L. Tankova ◽  
E. L. Iskakova ◽  
T. N. Golovach ◽  
...  
Keyword(s):  
Raw Materials ◽  
Farm Animals ◽  
Animal Origin ◽  
Enzyme Preparations ◽  
Global Trends ◽  
Antigenic Activity ◽  
The Republic ◽  
Protein Components ◽  
Hydrolysis Of ◽  
Plant Sources

. The article provides an assessment of the dairy farming need in the Russian Federation and the Republic of Belarus in calves feed. The main global trends aimed at providing young animals with high-quality food means are considered. Various variants of directed hydrolysis of calf milk replacer (CMR) protein components intended for feeding young animals in the first months of life are analyzed. The possibilities of reducing the soy proteins antigenic activity, which are widely used at present in the CMR formulations for feeding young farm animals, are discussed. The results of experimental work and patents are presented, which describe the most widely used approaches to the production of enzymatic hydrolysates of proteins with desired properties, as well as the assessment of their biological activity and immunochemical properties. The issues of using various enzyme preparations of bacterial, fungal and animal origin for hydrolysis of colostrum proteins and plant sources of protein raw materials for the CMR production are considered.

scholarly journals A New Opaque Variant of Maize by a Single Dominant RNA-Interference-Inducing Transgene

Genetics ◽  
2003 ◽  
Vol 165 (1) ◽  
pp. 387-397 ◽  
Author(s):  
Gregorio Segal ◽  
Rentao Song ◽  
Joachim Messing
Keyword(s):  
Rna Interference ◽  
Antisense Rna ◽  
Gene Families ◽  
Small Interfering Rnas ◽  
Dominant Phenotype ◽  
Main Protein ◽  
Protein Components ◽  
Storage Protein Genes ◽  
Zein Genes ◽  
Nutritional Imbalance

Abstract In maize, α-zeins, the main protein components of seed stores, are major determinants of nutritional imbalance when maize is used as the sole food source. Mutations like opaque-2 (o2) are used in breeding varieties with improved nutritional quality. However, o2 works in a recessive fashion by affecting the expression of a subset of 22-kD α-zeins, as well as additional endosperm gene functions. Thus, we sought a dominant mutation that could suppress the storage protein genes without interrupting O2 synthesis. We found that maize transformed with RNA interference (RNAi) constructs derived from a 22-kD zein gene could produce a dominant opaque phenotype. This phenotype segregates in a normal Mendelian fashion and eliminates 22-kD zeins without affecting the accumulation of other zein proteins. A system for regulated transgene expression generating antisense RNA also reduced the expression of 22-kD zein genes, but failed to give an opaque phenotype. Therefore, it appears that small interfering RNAs not only may play an important regulatory role during plant development, but also are effective genetic tools for dissecting the function of gene families. Since the dominant phenotype is also correlated with increased lysine content, the new mutant illustrates an approach for creating more nutritious crop plants.

Differential staining of crystalline arrays of outer mitochondrial membrane channels

1983 ◽  
Vol 41 ◽  
pp. 444-445
Author(s):  
Carmen A. Mannella ◽  
Joachim Frank
Keyword(s):  
Mitochondrial Membrane ◽  
Differential Staining ◽  
Mitochondrial Outer Membrane ◽  
Outer Mitochondrial Membrane ◽  
Mitochondrial Channels ◽  
Outer Membranes ◽  
Main Protein ◽  
Protein Components ◽  
Regular Arrays

The mitochondrial outer membrane contains pore-forming polypeptides (Mr⋍= 30,000) which are its main protein components in plants and fungi. Outer membranes (OM) isolated from Neurospora mitochondria often contain extended regular arrays of subunits with stain-accumulating centers 2-3 nm in diameter. That these subunits are the mitochondrial channels has been established immunologically. Antibodies against the predominant 31-kDa OM polypeptide of Neurospora (a) prevent in vitro insertion of OM channels into bilayers and (b) preferentially bind to the crystalline membranes in OM fractions.Planar projections of individual OM channel layers have been reconstructed from electron micrographs of negatively stained crystalline vesicles by Fourier filtration. In the usual array (Fig. 1a) the unit cell is a parallelogram which can hold six stain centers (putative pore openings) arranged in a hexagon with p2 symmetry. There are large pore-free areas in these arrays (* in Fig. 1a) which are likely composed of phospholipid, since they disappear when the membranes are treated with phospholipase A2 (Fig. 1b).

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