scholarly journals ELECTRON MICROSCOPIC AND BIOCHEMICAL CHARACTERIZATION OF COLLAGEN IN BLATTARIAN INSECTS

1967 ◽  
Vol 33 (2) ◽  
pp. 385-393 ◽  
Author(s):  
Elvin Harper ◽  
Sam Seifter ◽  
Berta Scharrer
Keyword(s):  
Trichloroacetic Acid ◽  
Biochemical Characterization ◽  
Corpus Allatum ◽  
Corpus Cardiacum ◽  
Guanidinium Chloride ◽  
Concentrated Solutions ◽  
Electron Microscopic ◽  
Bacterial Collagenase ◽  
Leucophaea Maderae

The occurrence of collagen in the cockroach Leucophaea maderae has been demonstrated by electron optical and biochemical techniques. Electron micrographs of tissues of this and a related species (Blaberus craniifer) are presented and they show that collagenous-type fibers occur in the stroma of nonneural as well as neural organs of these insects. Hydroxyproline and hydroxylysine, amino acids considered to be "markers" for collagen, have been shown to be present in proteins extracted from material rich in neuroglandular tissue (corpus cardiacum plus corpus allatum). Trimmed carcasses of Leucophaea maderae have been shown to contain a protein or proteins soluble in hot trichloroacetic acid, with compositional characteristics similar to those of collagens in general, including diagnostic proportions of glycine, proline, hydroxyproline, and hydroxylysine. This collagen is not soluble in dilute acetic acid or in concentrated solutions of guanidinium chloride. It is measurably digested by bacterial collagenase.

scholarly journals Biochemical characterization of guanidinium chloride-soluble dentine collagen from lathyritic-rat incisors

1979 ◽  
Vol 181 (3) ◽  
pp. 667-676 ◽  
Author(s):  
M Wohllebe ◽  
D J Carmichael
Keyword(s):  
Biochemical Characterization ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Neutral Salt ◽  
Guanidinium Chloride ◽  
Lysine Residues ◽  
Cross Links ◽  
Lysine Hydroxylation

alpha- and beta-Chains were isolated by sequential ion-exchange and gel-filtration chromatography of guanidinium chloride-soluble dentine collagen obtained from Tris/NaCl-extracted EDTA-demineralized lathyritic-rat incisors. The alpha-chains were identified as alpha 1 I and alpha 2 by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and amino acid analysis of the intact chains and their CNBr peptides. The dentine alpha-chains exhibited higher lysine hydroxylation and phosphate content, but lower hydroxylysine glycosylation, than alpha-chains from skin. Increased lysine hydroxylation was observed in the helical sequences. The alpha 1 I/alpha 2 ratio was approx. 3:1, and was presumably due to the presence of (alpha 1 I)3 molecules along with (alpha 1 I)2 alpha 2 molecules as shown recently for neutral-salt-soluble dentine collagen [Wohllebe & Carmichael (1978) Eur. J. Biochem. 92, 183–188]. In the borohydride-reduced beta 11- and beta 12-chains from guanidinium chloride-soluble dentine collagen, the reduced cross-links hydroxylysinohydroxynorleucine and hydroxylysinonorleucine were present. A higher proportion of hydroxylysinonorleucine in the reduced beta 12-chain probably reflects differences in extent of hydroxylation of specific lysine residues of the alpha 1 I- and alpha 2-chains.

Gastrin/CCK-like immunoreactivity in the corpus cardiacum-corpus allatum complex of the cockroach Leucophaea maderae

1987 ◽  
Vol 248 (3) ◽  
pp. 595-598 ◽  
Author(s):  
GeorgN�rgaard Hansen ◽  
BenteLangvad Hansen ◽  
Berta Scharrer
Keyword(s):  
Corpus Allatum ◽  
Corpus Cardiacum ◽  
Leucophaea Maderae

Electron Microscopic and Biochemical Characterization of Fraction I Protein

Science ◽  
1965 ◽  
Vol 150 (3703) ◽  
pp. 1598-1601 ◽  
Author(s):  
R. Haselkorn ◽  
H. Fernandez-Moran ◽  
F. J. Kieras ◽  
E. F. J. van Bruggen
Keyword(s):  
Biochemical Characterization ◽  
Electron Microscopic ◽  
Fraction I Protein ◽  
Fraction I

scholarly journals Biophysical characterization of Artemia salina (L.) extracellular haemoglobins

1981 ◽  
Vol 193 (1) ◽  
pp. 353-359 ◽  
Author(s):  
E J Wood ◽  
C Barker ◽  
L Moens ◽  
W Jacob ◽  
J Heip ◽  
...  
Keyword(s):  
High Speed ◽  
Artemia Salina ◽  
Low Ph ◽  
Sedimentation Equilibrium ◽  
Guanidinium Chloride ◽  
Electron Microscopic ◽  
Biophysical Characterization ◽  
Molecular Weights ◽  
Dimeric Model

Sedimentation coefficients (s0 20,w) of 11.57 +/- 0.10 S and 11.52 +/- 0.09 S were assigned for Artemia salina (L.) extracellular haemoglobins II and III respectively. These values are not significantly different. The molecular weights, M0w and M0z, of the native haemoglobins as determined by the high-speed sedimentation-equilibrium method were for haemoglobin II 239 400 +/- 7200 and 240 400 +/- 2600 respectively, and for haemoglobin III 216 300 +/- 6500 and 219 300 +/- 4500 respectively. The observed increase of Mapp. with concentration suggested that association was occurring over the concentration range investigated. Exposure of haemoglobin II to either 6 M-guanidinium chloride or to low pH (pH 4) resulted in dissociation to units of approximately half the size of the native protein, with molecular weights approx. 115 000. Electron-microscopic observations indicated a molecular structure composed of two stacked lobed discs. These results strongly support the dimeric model for Artemia haemoglobins proposed by Moens & Kondo [(1978) Eur. J. Biochem. 82, 65-72].

Electron Microscopic Detection and Characterization of Nonhuman Primate Enteric Viruses

1982 ◽  
Vol 40 ◽  
pp. 306-307
Author(s):  
G. C. Smith ◽  
R. L. Heberling ◽  
S. S. Kalter
Keyword(s):  
Electron Microscopy ◽  
Animal Model ◽  
Nonhuman Primate ◽  
Clinical Condition ◽  
Intestinal Tract ◽  
Enteric Viruses ◽  
Electron Microscopic ◽  
Microscopic Detection

A number of viral agents are recognized as and suspected of causing the clinical condition “gastroenteritis.” In our attempts to establish an animal model for studies of this entity, we have been examining the nonhuman primate to ascertain what viruses may be found in the intestinal tract of “normal” animals as well as animals with diarrhea. Several virus types including coronavirus, adenovirus, herpesvirus, and picornavirus (Table I) were detected in our colony; however, rotavirus, astrovirus, and calicivirus have not yet been observed. Fecal specimens were prepared for electron microscopy by procedures reported previously.

The Immuno-Electron Microscopic Localization of the Mo-Fe Protein Component of Nitrogenase in Cells of Azotobacter Vinelandii

1973 ◽  
Vol 31 ◽  
pp. 574-575
Author(s):  
J. T. Stasny ◽  
R. C. Burns ◽  
R. W. F. Hardy
Keyword(s):  
Cellular Localization ◽  
Direct Evidence ◽  
Azotobacter Vinelandii ◽  
Intracellular Localization ◽  
Protein Component ◽  
Electron Microscopic ◽  
Thin Sections ◽  
Fe Protein ◽  
Intracytoplasmic Membranes

Structure-functlon studies of biological N2-fixation have correlated the presence of the enzyme nitrogenase with increased numbers of intracytoplasmic membranes in Azotobacter. However no direct evidence has been provided for the internal cellular localization of any nitrogenase. Recent advances concerned with the crystallizatiorTand the electron microscopic characterization of the Mo-Fe protein component of Azotobacter nitrogenase, prompted the use of this purified protein to obtain antibodies (Ab) to be conjugated to electron dense markers for the intracellular localization of the protein by electron microscopy. The present study describes the use of ferritin conjugated to goat antitMo-Fe protein immunoglobulin (IgG) and the observations following its topical application to thin sections of N2-grown Azotobacter.

Plant Pathology Diagnosed by X-Ray Microanalysis

1987 ◽  
Vol 45 ◽  
pp. 974-975
Author(s):  
J. H. Resau ◽  
N. Howell ◽  
S. H. Chang
Keyword(s):  
Electron Microscopy ◽  
Plant Pathology ◽  
Biochemical Characterization ◽  
Nutrient Deficiency ◽  
Green Leaf ◽  
Parasitic Infestation ◽  
X Ray

Spinach grown in Texas developed “yellow spotting” on the peripheral portions of the leaves. The exact cause of the discoloration could not be determined as there was no evidence of viral or parasitic infestation of the plants and biochemical characterization of the plants did not indicate any significant differences between the yellow and green leaf portions of the spinach. The present study was undertaken using electron microscopy (EM) to determine if a micro-nutrient deficiency was the cause for the discoloration.Green leaf spinach was collected from the field and sent by express mail to the EM laboratory. The yellow and equivalent green portions of the leaves were isolated and dried in a Denton evaporator at 10-5 Torr for 24 hrs. The leaf specimens were then examined using a JEOL 100 CX analytical microscope. TEM specimens were prepared according to the methods of Trump et al.

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