Wet degradation of keratin proteins: linking amino acid, elemental and isotopic composition

2014 ◽  
Vol 28 (19) ◽  
pp. 2121-2133 ◽  
Author(s):  
I. C. C. von Holstein ◽  
K. E. H. Penkman ◽  
E. E. Peacock ◽  
M. J. Collins
Keyword(s):  
Amino Acid ◽  
Isotopic Composition ◽  
Keratin Proteins

Amino acid nitrogen isotopic composition patterns in lacustrine sedimenting matter

2013 ◽  
Vol 121 ◽  
pp. 328-338 ◽  
Author(s):  
Dörte Carstens ◽  
Moritz F. Lehmann ◽  
Thomas B. Hofstetter ◽  
Carsten J. Schubert
Keyword(s):  
Amino Acid ◽  
Isotopic Composition ◽  
Amino Acid Nitrogen ◽  
Nitrogen Isotopic Composition

3-Amino-5-Hydroxybenzoic Acid in Antibiotic Biosynthesis. IX. The Status of Reduced Derivatives in Mitomycin Biosynthesis

1987 ◽  
Vol 40 (5) ◽  
pp. 1011 ◽  
Author(s):  
RW Rickards ◽  
V Rukachaisirikul
Keyword(s):  
Amino Acid ◽  
Isotopic Composition ◽  
Antibiotic Biosynthesis ◽  
Hydroxybenzoic Acid ◽  
The Status ◽  
Metabolic Precursors ◽  
Hydroxybenzyl Alcohol

The addition of (methylene-2H2)-3-amino-5-hydroxybenzyl alcohol (8) hydrochloride to growing cultures of Streptomyces verticillatus inhibits production of the mitomycin antibiotic porfiromycin (2) by the microorganism. No incorporation of deuterium into porfiromycin occurs, and the isotopic composition of the alcohol recovered from the fermentation is unchanged. The significance of these results with regard to the immediate metabolic precursors of 3-amino-5-hydroxybenzoic acid (3) and the reduction stages involved in the established conversion of this amino acid into mitomycins are discussed.

Nautilus hard parts: a study of the mineral and organic constitutents

Paleobiology ◽  
1984 ◽  
Vol 10 (2) ◽  
pp. 268-279 ◽  
Author(s):  
H. A. Lowenstam ◽  
W. Traub ◽  
S. Weiner
Keyword(s):  
Amino Acid ◽  
Isotopic Composition ◽  
Protein Complexes ◽  
Organic Matrix ◽  
Tendon Sheath ◽  
Evolutionary Trend ◽  
X Ray Diffraction ◽  
Shell Wall ◽  
X Ray ◽  
Tube Shell

The mineralized hard parts of Nautilus, including the mandibles, statoconia, and uroliths, are more complex with respect to ultrastructure, mineralogy, trace element, and isotopic composition than was previously recognized. X-ray diffraction and amino acid composition analyses of the organic structural hard parts (siphuncle tube, shell wall and septum organic matrix, mandibles, and muscle tendon sheath) show that two different chitin-protein complexes are utilized by Nautilus. The mandible mineral hard parts are particularly complex, with five different minerals present in various locations. A comparison of the statoconia of Nautilus species with the statoliths of dibranchian cephalopods reveals an evolutionary trend in which carbonate is substituted for phosphate. This study also shows that Nautilus uses a number of different crystal-forming processes for constructing its hard parts. The data presented here provide a broad spectrum of information, which, when applied to the fossil counterparts, can be utilized for improving our understanding of ancient nautiloid biology.

scholarly journals The Proteins of the Keratin Component of Bird?s Beaks

1976 ◽  
Vol 29 (6) ◽  
pp. 467 ◽  
Author(s):  
MJ Frenkel ◽  
JM Gillespie
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Major Protein ◽  
Major Fraction ◽  
Amino Acid Compositions ◽  
Molecular Weights ◽  
Isoelectric Points ◽  
Related Proteins ◽  
Keratin Proteins ◽  
Similar Amino Acid

Birds' beaks have an outer shell of hard keratin which consists almost entirely of proteins which are very rich in glycine [about 30 residues per 100 residues (residues %)], contain moderate levels of tyrosine and serine (each about 8 residues %), and which have relatively low contents of cystine (about 2�5 residues %), lysine, histidine, isoleucine and methionine. Major protein fractions in the S-carboxymethyl form isolated from the beaks of 'six different orders of birds have similar amino acid compositions, isoelectric points (pH 4�2-4�9) and molecular weights (13 000--14 500). Detailed chromatographic electrophoretic and compositional studies of the proteins of kookaburra beak reveal them to be a family of closely related proteins with only limited heterogeneity, in contrast to mammalian keratin systems. The major kookaburra beak fraction is similar in overall composition and molecular weight to fowl epidermal scale, kookaburra claw and turtle scute proteins and shows some resemblance to reptile claw protein. Beaks also contain small amounts of protein which are distinctly different from the major fraction but which resemble feather keratin proteins in composition and size.

The staining pattern of the tropomyosin sequence is displayed in a new paracrystal

1986 ◽  
Vol 44 ◽  
pp. 150-151
Author(s):  
M.K. Lamvik ◽  
L.L. Klatt
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Staining Pattern ◽  
Banding Patterns ◽  
Mass Thickness ◽  
New Form

Tropomyosin paracrystals have been used extensively as test specimens and magnification standards due to their clear periodic banding patterns. The paracrystal type discovered by Ohtsuki1 has been of particular interest as a test of unstained specimens because of alternating bands that differ by 50% in mass thickness. While producing specimens of this type, we came across a new paracrystal form. Since this new form displays aligned tropomyosin molecules without the overlaps that are characteristic of the Ohtsuki-type paracrystal, it presents a staining pattern that corresponds to the amino acid sequence of the molecule.

Electron probe x-ray microanalysis and electron microscopy of amino acid absorption and transport by the small intestine: inhibition by chemical poisons and correlation to the elemental composition of the epithelial cells

1986 ◽  
Vol 44 ◽  
pp. 134-135
Author(s):  
A. J. Tousimis
Keyword(s):  
Small Intestine ◽  
Amino Acid ◽  
Epithelial Cells ◽  
Elemental Composition ◽  
Isotope Labeling ◽  
Structural Components ◽  
X Ray ◽  
Human Small Intestine ◽  
Transport Studies

The elemental composition of amino acids is similar to that of the major structural components of the epithelial cells of the small intestine and other tissues. Therefore, their subcellular localization and concentration measurements are not possible by x-ray microanalysis. Radioactive isotope labeling: I131-tyrosine, Se75-methionine and S35-methionine have been successfully employed in numerous absorption and transport studies. The latter two have been utilized both in vitro and vivo, with similar results in the hamster and human small intestine. Non-radioactive Selenomethionine, since its absorption/transport behavior is assumed to be the same as that of Se75- methionine and S75-methionine could serve as a compound tracer for this amino acid.

Immunoelectron microscope detection of C-type natriuretic peptide in normal human atrial tissue

1993 ◽  
Vol 51 ◽  
pp. 388-389
Author(s):  
Chi-Ming Wei ◽  
Margaret Hukee ◽  
Christopher G.A. McGregor ◽  
John C. Burnett
Keyword(s):  
Amino Acid ◽  
Natriuretic Peptide ◽  
Vascular Tone ◽  
Cardiac Tissue ◽  
Ring Structure ◽  
Terminal Amino Acid ◽  
Amino Acid Peptide ◽  
Normal Human ◽  
Terminal Amino ◽  
The Brain

C-type natriuretic peptide (CNP) is a newly identified peptide that is structurally related to atrial (ANP) and brain natriuretic peptide (BNP). CNP exists as a 22-amino acid peptide and like ANP and BNP has a 17-amino acid ring formed by a disulfide bond. Unlike these two previously identified cardiac peptides, CNP lacks the COOH-terminal amino acid extension from the ring structure. ANP, BNP and CNP decrease cardiac preload, but unlike ANP and BNP, CNP is not natriuretic. While ANP and BNP have been localized to the heart, recent investigations have failed to detect CNP mRNA in the myocardium although small concentrations of CNP are detectable in the porcine myocardium. While originally localized to the brain, recent investigations have localized CNP to endothelial cells consistent with a paracrine role for CNP in the control of vascular tone. While CNP has been detected in cardiac tissue by radioimmunoassay, no studies have demonstrated CNP localization in normal human heart by immunoelectron microscopy.

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