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.

Isolation and characterization of pepsin-solubilized human basement membrane (type IV) collagen peptides

Biochemistry ◽  
1983 ◽  
Vol 22 (21) ◽  
pp. 4940-4948 ◽  
Author(s):  
Robert S. MacWright ◽  
Virginia A. Benson ◽  
Katherine T. Lovello ◽  
Michel Van der Rest ◽  
Peter P. Fietzek
Keyword(s):  
Basement Membrane ◽  
Type Iv Collagen ◽  
Collagen Peptides ◽  
Type Iv ◽  
Isolation And Characterization ◽  
Membrane Type

viking: identification and characterization of a second type IV collagen in Drosophila

Gene ◽  
1997 ◽  
Vol 198 (1-2) ◽  
pp. 17-25 ◽  
Author(s):  
Sukkid Yasothornsrikul ◽  
Wendy J Davis ◽  
Gabrielle Cramer ◽  
Deborah A Kimbrell ◽  
Charles R Dearolf
Keyword(s):  
Type Iv Collagen ◽  
Type Iv ◽  
Identification And Characterization

scholarly journals Purification and characterization of type IV collagen from mouse kidney.

1986 ◽  
Vol 34 (2) ◽  
pp. 789-797 ◽  
Author(s):  
TSUTOMU OIKAWA ◽  
TAKAO IWAGUCHI ◽  
MIKIO KIMURA ◽  
AKIO MATSUZAWA
Keyword(s):  
Type Iv Collagen ◽  
Mouse Kidney ◽  
Purification And Characterization ◽  
Type Iv

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 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.

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