Preliminary Characterization of Resilin Isolated from the Cockroach, Periplaneta Americana

1992 ◽  
Vol 292 ◽  
Author(s):  
Elizabeth Craig Lombardi ◽  
David L. Kaplan
Keyword(s):  
Mechanical Properties ◽  
Amino Acid ◽  
Amino Acid Analysis ◽  
Periplaneta Americana ◽  
Insect Cuticle ◽  
Oligonucleotide Probes ◽  
Protein Matrix ◽  
Tryptic Fragment ◽  
Good Agreement

AbstractWe would like to mimic the mechanical properties of animal systems for the development of novel materials. Insect cuticle serves as one source of inspiration for the design of these materials. Cuticle is composed of chitin embedded in a protein matrix which may also contain plasticizers, fillers, crosslinkers, and minerals. The specific properties of the cuticle depend on the type, amount and interactions between each component. We are renewing the investigation of the elastic cuticle, resilin. Resilin, a protein-based elastomer first described in the early 1960s, has properties which have been reported to be most like those of ideal rubbers. We have examined resilin isolated from the prealar arms of the cockroach, Periplaneta americana. The results of amino acid analysis are in good agreement with earlier data reported for resilin. A series of tryptic fragments have been isolated and sequenced. These peptides have been used for the design of oligonucleotide probes for the identification of the gene(s) from a teneral cockroach cDNA library. A biopolymer, based on one tryptic fragment, has been designed and synthesized. We are continuing to treat resilin with residue specific proteases in order to map the resilin protein.

scholarly journals Purification and characterization of human neuropeptide Y from adrenal-medullary phaeochromocytoma tissue

1984 ◽  
Vol 219 (3) ◽  
pp. 699-706 ◽  
Author(s):  
R Corder ◽  
P C Emson ◽  
P J Lowry
Keyword(s):  
Amino Acid ◽  
Neuropeptide Y ◽  
Amino Acid Analysis ◽  
Gel Filtration ◽  
Exchange Chromatography ◽  
Carboxypeptidase Y ◽  
Purification And Characterization ◽  
Reverse Phase ◽  
Tryptic Fragment

Human neuropeptide Y was isolated from acid extracts of adrenal-medullary phaeochromocytoma tissue. After (NH4)2SO4 fractionation, the neuropeptide Y-like immunoreactivity was purified from the resolubilized 80%-saturation-(NH4)2SO4 peptide-rich precipitate, by gel filtration, cation-exchange chromatography and reverse-phase high-pressure liquid chromatography. Amino acid analysis of the peptide revealed a composition almost identical with that of the pig peptide, the exception being the loss of one leucine residue and its replacement with methionine. Tryptic digestion of the peptide and subsequent amino acid analysis of the fragments further confirmed the identity of the peptide. Carboxypeptidase Y digestion of the (1-19)-peptide tryptic fragment has shown the methionine to be located at position 17 in human neuropeptide Y.

scholarly journals The heparin–protein complex of ox liver capsule. Isolation and chemical characterization

1969 ◽  
Vol 112 (2) ◽  
pp. 167-172 ◽  
Author(s):  
A Serafini-Fracassini ◽  
J J Durward ◽  
L. Floreani
Keyword(s):  
Amino Acid ◽  
Column Chromatography ◽  
Catalytic Hydrogenation ◽  
Protein Complex ◽  
Amino Acid Analysis ◽  
Chemical Characterization ◽  
Isolation And Purification ◽  
Liver Capsule ◽  
Heparin Fractions ◽  
Good Agreement

1. A procedure for the isolation and purification of the heparin–protein complex from ox liver capsule, based on the solubility properties of mucopolysaccharide–cetylpyridinium complexes, is described. 2. The yield of the heparin–protein complex with this method averages 35mg./100g. of dry ox liver capsule. 3. The results of analyses on the polysaccharide show good agreement with values previously published for purified heparin fractions. 4. The amino acid analysis of the protein component shows several similarities to that of chondromucoprotein. 5. The results of β-carbonyl elimination, either with or without catalytic hydrogenation, and column chromatography after β-elimination, show that the polysaccharide is covalently bound to the protein.

FIBRINOGEN BIRMINGHAM; A NEW CONGENITAL HETERODIMERIC DYSFIBRINOGENEMIA WITH DEFECTIVE FIBRINOPEPTIDE A RELEASE (Aα 16 Arg→His)

1987 ◽  
Author(s):  
K R Siebenlist ◽  
J T Prchal ◽  
M W Masesson
Keyword(s):  
Amino Acid ◽  
Amino Acid Analysis ◽  
Hplc Analysis ◽  
Biochemical Characterization ◽  
Clinical Manifestations ◽  
Severe Bleeding ◽  
Fibrinopeptide A ◽  
History Of ◽  
Bleeding Episodes

Aα 16 Arg→His substitutions are common forms of congenital dysfibrinogenemias. Clinical manifestations range from asymptomatic to moderate hemorrhagic tendencies. Biochemical characterization of one such heterozygotic individual (Fibrinogen Louisville, Galanakis, etal. Ann NY Acad Sci 408:644,1983) indicated that only homodimeric fibrinogen molecules (i.e., containing either normal or abnormal Aα chains) were present. We isolated fibrinogen from the plasma of a 23 year old patient with a history of easy bruising and several recent moderate to severe bleeding episodes. Coagulability with reptilase was 677 (65-70%; n=5) whereas with thrombin (Ha) it approached 100%, depending directly upon the time of incubation with enzyme. HPLC analysis of Ila-induced fibrinopeptide release demonstrated the presence of an abnormal A-peptide (A*), amounting to 50% of the total, which was released more slowly than the normal A-peptide (A). Amino acid analysis of A* demonstrated the absence of Arg and the presence of His. Carboxypeptidase digestion confirmed the structure of A* as Aα 16 Arg-→ His. The clot and the soluble clot liquor resulting from reptilase treatment were separated and each was then further treated with Ilato release A*. HPLC analysis indicated that 31% of the total A* present in the sample was associated with the reptilase clot and 697 remained in the clot liquor. This distribution of A* suggests that Fibrinogen Birmingham, unlike Fibrinogen Louisville, contains heterodimeric molecules that are incorporated into the reptilase clottable fraction. This finding is consistent with a process of random hepatic assembly of dimeric fibrinogen molecules in a heterozygotic individual.

scholarly journals Bakerian lecture - Amino-acid analysis and the structure of proteins

1942 ◽  
Vol 131 (863) ◽  
pp. 136-160 ◽  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Analysis ◽  
Nutritive Value ◽  
Analytical Data ◽  
Seed Proteins ◽  
Decomposition Products ◽  
First Time ◽  
Structure Of Proteins

In recent years the X-ray crystallographers have made remarkable advances in the interpretation of protein structure, and it is becoming more and more evident that a stage has been reached when their views need to be reconciled with data obtained from accurate amino-acid analysis of the proteins concerned. In all too many cases these data are, unfortunately, not yet available, and the reason why the analyst cannot supply them at short notice is due not so much to the com­plexity of the problem—which he has never sought to minimize—but to the fact that many of the more important methods of analysis in current use are an inheritance from an earlier period when such accuracy as is now demanded would have been considered almost impossible of achievement. From about 1840 until 1900, following the lead given by Liebig and later by Ritthausen, the attention of protein chemists was centred chiefly on the prepara­tion and characterization of various animal and seed proteins; as substances of physiological interest their enzymic digestion products were studied in elaborate detail by Kühne, but little attention was paid to the ultimate decomposition products, the amino-acids, in spite of the fact that Ritthausen as early as 1872 had pointed out that the proportions in which these occur might be characteristic of the protein concerned. The enunciation by Hofmeister and Fischer of the peptide hypothesis in 1901 emphasized for the first time the fundamental importance of the amino-acids, and a most fruitful period followed in which attention became almost exclusively focused on these products. Under the inspiring leadership of Fischer himself great improvements were effected in the separation and identification of the amino-acids, so that by about 1915 reasonably good analyses were available for most of the better-known proteins. Though far from complete, the analytical data showed quite clearly that proteins could differ widely in composition, and in many cases it was possible to correlate composition with nutritive value. Such an aim was, indeed, the incentive behind much of the work of this period.

Partial characterization of the heteropolysaccharide associated with the 7S domain of type IV collagen from placenta

1987 ◽  
Vol 65 (5) ◽  
pp. 501-506 ◽  
Author(s):  
James R. A. Leushner
Keyword(s):  
Sialic Acid ◽  
Amino Acid ◽  
Chemical Analysis ◽  
Amino Acid Analysis ◽  
Molecular Sieve ◽  
Type Iv Collagen ◽  
Relative Mass ◽  
Type Iv ◽  
Structure Formula

A major heteropolysaccharide fraction was isolated from the 7S domain of human placental type IV collagen. Analyses revealed that it was an asparagine-linked oligosaccharide. Characterization using molecular sieve chromatography, exoglycosidase and endoglycosidase digestion, and chemical analysis suggested a bianternnary complex with the following structure:[Formula: see text]A microheterogeneity was noted with respect to the addition of the fucose and sialic acid residues. Analysis of component polypeptides of the 7S fraction following endoglycosidase treatment suggested that the most obvious site of heteropolysaccharide attachment was in a polypeptide of relative mass 40 000. Amino acid analysis of this isolated polypeptide indicated that it was rich in collagenous sequences and also contained half-cystine residues.

Round-Hole-Fiber Distribution in Hydrophilidae Cuticle and Biomimetic Research

2005 ◽  
Vol 288-289 ◽  
pp. 433-436
Author(s):  
Bin Chen ◽  
Xiang He Peng ◽  
Jing Hong Fan
Keyword(s):  
Mechanical Properties ◽  
Fracture Toughness ◽  
Ultimate Strength ◽  
Composite Laminate ◽  
Insect Cuticle ◽  
Round Hole ◽  
Fiber Distribution ◽  
Protein Matrix ◽  
Sem Observation

Insect cuticle possesses excellent mechanical properties, such as strength, stiffness and fracture toughness, which are closely related to its elaborate microstructures optimized through centuries’ evolution. SEM observation on Hydrophilidae cuticle shows a kind of biocomposite consisting of chitin-fiber plies and protein matrix, and the chitin-fiber plies are composed of several special arrangements. The observation also shows that there are many holes in the cuticle and the fibers passing along the brims of the holes round the holes continuously. Making use of such microstructure, a kind of biomimetic composite laminate with round-hole-fiber distribution is fabricated with preformed-hole method. The ultimate strength of the composite laminate is investigated and compared with that of the composite laminate with a hole drilled. It shows that the ultimate strength of the former is distinctly higher than that of the latter.

scholarly journals Proteolytic Characterization of Lactobacillus delbrueckii ssp. bulgaricus Strains by the o-Phthaldialdehyde Test and Amino Acid Analysis

1991 ◽  
Vol 74 (2) ◽  
pp. 398-403 ◽  
Author(s):  
Craig J. Oberg ◽  
Bart C. Weimer ◽  
Lynn V. Moyes ◽  
Rodney J. Brown ◽  
Gary H. Richardson
Keyword(s):  
Amino Acid ◽  
Amino Acid Analysis ◽  
Lactobacillus Delbrueckii
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