Isolation, ultrastructure, and partial characterization of collagen from the perineurium of the Florida lobster, Panulirus argus

1991 ◽  
Vol 69 (8) ◽  
pp. 531-536
Author(s):  
Roy J. Baerwald ◽  
Lura C. Williamson ◽  
E. Stevens ◽  
C. Rike ◽  
S. Trabanino ◽  
...  
Keyword(s):  
Amino Acid ◽  
Protein Content ◽  
Type I Collagen ◽  
Carbohydrate Content ◽  
Panulirus Argus ◽  
Computer Assisted ◽  
Type I ◽  
X Ray Diffraction ◽  
X Ray ◽  
Fibril Diameter

Highly concentrated extracellular filaments in the perineurium of the Florida spiny lobster, Panulirus argus, were isolated using ultracentrifugation and linear sucrose gradients. The pellet obtained was highly enriched for the filaments as observed by transmission electron microscopy. Fibril diameter and axial periodicity measurements were obtained from filaments positively and negatively stained with uranyl acetate. A period between 14.0 and 25.0 nm and an average fibril diameter of 15.0 nm were observed. The filaments proved resistant to solubilization by most conventional agents and by several collagenases. NaOH (0.1 M at 100 °C) safely dissolved the filaments for measurements of protein content by the Lowry method and carbohydrate content with anthrone reagent. These tests revealed a protein content of ≈ 84% and a high carbohydrate content of ≈ 15%. Polyacrylamide electrophoresis of an acid-pepsin filament extract revealed a highly concentrated band (approximately 100 000) corresponding to the α-1 and α-2 bands of vertebrate type I collagen. Wide angle X-ray diffraction yielded meridional reflections that confirmed the filaments as collagen when compared with mammalian collagen X-ray diffraction. The amino acid composition was determined with a computer-assisted Beckman amino acid analyzer, which showed a glycine content of 279 residues/1000. Hydroxylysine and hydroxyproline were present in lower concentrations than expected.Key words: perineurium, lobster, collagen, extracellular matrix.

A new model for packing of type-I collagen molecules in the native fibril

1981 ◽  
Vol 1 (10) ◽  
pp. 801-810 ◽  
Author(s):  
Karl A. Piez ◽  
Benes L. Trus
Keyword(s):  
Type I Collagen ◽  
Hexagonal Lattice ◽  
Three Dimensional ◽  
Equatorial Region ◽  
Type I ◽  
X Ray Diffraction ◽  
X Ray ◽  
Left Handed ◽  
Crystal Model ◽  
Collagen Molecules

A specific fibril model is presented consisting of bundles of five-stranded microfibrils, which are usually disordered (except axially) but under lateral compression become ordered. The features are as follows (where D = 234 residues or 67 nm): (1) D-staggered collagen molecules 4.5 D long in the helical microfibril have a left-handed supercoil with a pitch of 400–700 residues, but microfibrils need not have helical symmetry. (2) Straight-tilted 0.5-D overlap regions on a near-hexagonal lattice contribute the discrete x-ray diffraction reflections arising from lateral order, while the gap regions remain disordered. (3) The overlap regions are equivalent, but are crystallographically distinguished by systematic displacements from the near-hexagonal lattice. (4) The unit cell is the same as in a recently proposed three-dimensional crystal model, and calculated intensities in the equatorial region of the x-ray diffraction pattern agree with observed values.

Heat Treatment Strengthens Human Dentin

2008 ◽  
Vol 87 (8) ◽  
pp. 762-766 ◽  
Author(s):  
M. Hayashi ◽  
E.V. Koychev ◽  
K. Okamura ◽  
A. Sugeta ◽  
C. Hongo ◽  
...  
Keyword(s):  
Heat Treatment ◽  
Stress Intensity ◽  
Type I Collagen ◽  
Type I ◽  
Third Molars ◽  
X Ray Diffraction ◽  
Intensity Factors ◽  
X Ray ◽  
Human Dentin ◽  
Triple Helices

The flexural strength of Type I collagen, the major organic component of human dentin, increases with heat. We hypothesized that human dentin can be strengthened by heating, which may help prevent fracture of non-vital teeth after restoration. Beam-shaped dentin specimens were obtained from the crowns of human third molars. The dentinal tubular orientations were arranged to run parallel or perpendicular to loading surfaces. The flexural and microtensile strengths of dentin in the parallel specimens were 2- to 2.4-fold greater after being heated between 110°C and 140°C for 1 hr. The stress intensity factors at fracture also increased after specimens were heated. The x-ray diffraction analyses suggested that shrinking of the lateral packing of the collagen triple-helices from 14 Å to 11 Å was the probable cause of the strengthening of heated dentin. We conclude that heat treatment strengthens human dentin.

The Effects of Different Hydroxyapatite/TiO2 Composite Coatings on Protein Expression of Osteoblast

2009 ◽  
Vol 610-613 ◽  
pp. 1104-1108 ◽  
Author(s):  
Jian Ye Han ◽  
Zhen Tao Yu ◽  
Lian Zhou
Keyword(s):  
Protein Expression ◽  
Type I Collagen ◽  
Composite Coatings ◽  
Type I ◽  
X Ray Diffraction ◽  
Rt Pcr ◽  
Chain Reaction ◽  
Compound Formation ◽  
X Ray ◽  
Polymerase Chain

Hydroxyapatite/TiO2 composite material was coated onto Ti25Nb3Mo2Sn3Zr (TLM) alloy substrate. To study the effects of hydroxyapatite/TiO2 composite coatings on bone-related protein expression, the osteoblast were cultured with composite coatings for different times. The phase transformation and compound formation of the HA/TiO2 coatings were investigated using XRD (X-ray diffraction). The mRNA expression of Type I collagen, alkaline phosphatase (ALP) and osteocalcin were studied by RT-PCR (reverse transcriptional polymerase chain reaction). The titania delayed the crystallization of HA. The mRNA expressions of Type I collagen are decreased as the increasing of TiO2 percentage. The mRNA expressions of osteocalcin are approached. The ALP expression on H4 coating (HA/TiO2 mol ration is 5) after the osteoblast cultured with composite coating for 6 days is the highest. The increasing of TiO2 amount decreases the bioactivity of the composite coatings.

HAp Protein Composites Formed by Hydrolysis of α-TCP

2005 ◽  
Vol 284-286 ◽  
pp. 39-42 ◽  
Author(s):  
Ahmed H. Touny ◽  
Paul W. Brown
Keyword(s):  
Type I Collagen ◽  
Isothermal Calorimetry ◽  
Protein Structures ◽  
Structural Proteins ◽  
Surrounding Tissue ◽  
Type I ◽  
X Ray Diffraction ◽  
X Ray ◽  
Hydrolysis Of ◽  
Aggressive Effect

Composite material composed of hydroxyapatite (HAp) and structural proteins, such as type I collagen or cross-linked gelatins, were synthesized at 37.4°C by hydrolysis of alpha tricalcium phosphate (α-TCP) in the presence of these protein structures. X-ray diffraction (XRD)and isothermal calorimetry were used as tools to evaluate the rate of HAp formation. Rates of HAp formation depend on protein structure. Gelatin enhances HAp formation while collagen delays it. Changes in pH during the hydrolysis α-TCP are unlikely to have an aggressive effect on the surrounding tissue. The presence of the protein improves the ductility of the HAp/protein composite but it decreases the tensile strength.

Axially Chiral Bis(α-amino Acid)s and Their Deamino Analogues. Synthesis and Configurational Assignment

1998 ◽  
Vol 63 (2) ◽  
pp. 211-221 ◽  
Author(s):  
Miloš Tichý ◽  
Luděk Ridvan ◽  
Miloš Buděšínský ◽  
Jiří Závada ◽  
Jaroslav Podlaha ◽  
...  
Keyword(s):  
Amino Acid ◽  
Nmr Spectra ◽  
Building Blocks ◽  
X Ray Diffraction ◽  
Amino Groups ◽  
X Ray ◽  
Configurational Assignment ◽  
Symmetry Properties ◽  
Axially Chiral ◽  
Polymeric Structures

The axially chiral bis(α-amino acid)s cis-2 and trans-2 as possible building blocks for polymeric structures of novel type of helicity were prepared. Their configuration has been determined by NMR spectroscopy and, in the case of the trans-isomer, confirmed by single-crystal X-ray diffraction. Analogous pair of stereoisomeric diacids cis-3 and trans-3, devoid of the amino groups, was also prepared and their configuration assigned. The observed differences in the NMR spectra of cis- and trans-isomers of 2 and 3 are discussed from the viewpoint of their different symmetry properties.

Assembly of type I collagen: fusion of fibril subunits and the influence of fibril diameter on mechanical properties

2000 ◽  
Vol 19 (5) ◽  
pp. 409-420 ◽  
Author(s):  
David L. Christiansen ◽  
Eric K. Huang ◽  
Frederick H. Silver
Keyword(s):  
Mechanical Properties ◽  
Type I Collagen ◽  
Type I ◽  
Fibril Diameter

The Effect of Different Methods to Pretreat Reed Pulp on the Crystallinity of Microcrystalline Cellulose

2014 ◽  
Vol 1056 ◽  
pp. 12-15 ◽  
Author(s):  
Wen Long Zhang ◽  
Wen Long Zhao ◽  
Ya Jie Dai
Keyword(s):  
Crystallite Size ◽  
Microcrystalline Cellulose ◽  
Average Crystallite Size ◽  
Comprehensive Analysis ◽  
Raw Material ◽  
Type I ◽  
X Ray Diffraction ◽  
X Ray ◽  
Dimethyl Acetamide ◽  
Crystal Type

Reed Pulp was Raw Material that Pretreated by Four Methods {ultrasonic, Microwave, N, N-Dimethyl Acetamide (DMAc) and Tetrahydrofuran (THF)}. Reed Microcrystalline Cellulose (MCC) was Prepared by the Dilute Hydrochloric Acid Hydrolysis from Pretreated Reed Pulp. the Influences of Pretreatment Methods on Crystalline Type, Crystallinity and Crystallite Size of MCC were Investigated by X-Ray Diffraction (XRD). the Results Showed that the Crystallinity of MCC with Four Pretreatment Methods was 68.45%, 62.28%, 63.21% and 69.56%, Respectively. the Average Crystallite Size of MCC Prepared by Hydrolysis after Pretreated by Dmac was the Largest. whereas, the Crystal Type of MCC was Not Changed, it was still the Cellulose Type I. Comprehensive Analysis Indicated that the Effects of MCC Prepared by Hydrolysis after Pretreated by Ultrasonic were the Best.

scholarly journals Synthesis, characterization, x-ray diffraction studies and biological activities of iron(III) and cobalt(II) complexes with alanine

2018 ◽  
Vol 6 (2) ◽  
pp. 132
Author(s):  
Shuaibu Musa ◽  
S O. Idris ◽  
A D. Onu
Keyword(s):  
Amino Acid ◽  
Biological Activities ◽  
Human Life ◽  
Molar Conductance ◽  
Biological Molecules ◽  
X Ray Diffraction ◽  
Monoclinic Crystal ◽  
X Ray ◽  
Metal Ligands ◽  
Elemental Analyses

The resulted complexes produced between Fe (III) and Co (II) with biological molecules like amino acids play an important role in human life. They can be used as bioactive compounds as well as in industries. Fe (III) and Co (II) complexes are synthesized with Alanine amino acid. The complexes were characterized by X-ray diffraction, magnetic suscetivility, elemental analysis (AAS), molar conductance, melting point, infrared and uv-visible spectrophotometry analyses. The elemental analyses were used to determine the chelation ratio, 1:3(metal: ligands) for iron (III) Alanine and 1:2 ratio for cobalt (II) Alanine. The molar conductivity of the complexes show that the complexes are not electrolytic in nature. The x-ray data suggest monoclinic crystal system for all the complexes with the exception of Co-alanine, which is hexagonal. The magnetic susceptivility and electronic spectra suggest the complexes are high spin with octahedral geometry.The complexes show enhance activity in comparable to the amino acid.  

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