An avian serum .alpha.1-glycoprotein, hemopexin, differing significantly in both amino acid and carbohydrate composition from mammalian (.beta.-glycoprotein) counterparts

Biochemistry ◽  
1986 ◽  
Vol 25 (21) ◽  
pp. 6555-6562 ◽  
Author(s):  
Valentina Goldfarb ◽  
Robert B. Trimble ◽  
Maria De Falco ◽  
Heng Liem ◽  
Sylvia A. Metcalfe ◽  
...  
Keyword(s):  
Amino Acid ◽  
Carbohydrate Composition

scholarly journals Tamm–Horsfall urinary glycoprotein. The chemical composition

1970 ◽  
Vol 120 (2) ◽  
pp. 417-424 ◽  
Author(s):  
A. P. Fletcher ◽  
A. Neuberger ◽  
Wendy A. Ratcliffe
Keyword(s):  
Amino Acid ◽  
Performic Acid ◽  
Acid Oxidation ◽  
Amino Acid Residues ◽  
Carbohydrate Composition ◽  
Thiol Groups ◽  
Terminal Amino Acid ◽  
Cystine Content ◽  
Terminal Amino ◽  
Urinary Glycoprotein

1. A revised amino acid and carbohydrate composition of human Tamm–Horsfall glycoprotein is presented. 2. No significant differences were obtained in the amino acid composition of Tamm–Horsfall glycoprotein isolated from patients with cystic fibrosis. 3. The glycoprotein was shown to possess a high half-cystine content of 1 per 11–12 amino acid residues, which has been confirmed by performic acid oxidation and S-alkylation with iodoacetate and iodoacetamide. No thiol groups were detected in the glycoprotein. 4. Treatment of the glycoprotein with 0.5m-sodium hydroxide at 4°C for 2 days did not release heterosaccharide material, which suggests that the predominant carbohydrate–protein linkages present are not of the O-glycosidic type. 5. No N-terminal amino acid was detected in the glycoprotein.

scholarly journals The isolation of ovomucoid variants differing in carbohydrate composition

1971 ◽  
Vol 123 (3) ◽  
pp. 399-405 ◽  
Author(s):  
J. G. Beeley
Keyword(s):  
Sialic Acid ◽  
Amino Acid ◽  
Acid Content ◽  
Deae Cellulose ◽  
Structure And Function ◽  
Inhibiting Activity ◽  
Carbohydrate Composition ◽  
Charge Heterogeneity ◽  
Sialic Acid Content ◽  
And Function

Three major and two minor species of ovomucoid were separated by chromatography on sulphoethyl-Sephadex. The predominant sialic acid-free species was further resolved into three fractions by DEAE-cellulose chromatography. Although all species of ovomucoid had closely similar trypsin-inhibiting activity, immunochemical properties and amino acid composition, they differ in carbohydrate composition. Wide variation was observed in the content of galactose, N-acetylglucosamine and sialic acid. Charge heterogeneity was related, in part, to variation in sialic acid content. The implications of variable carbohydrate composition for the structure and function of ovomucoid are discussed.

Preparation and fractionation of goat κ-casein: analysis of the glycan and peptide components

1978 ◽  
Vol 45 (2) ◽  
pp. 191-196 ◽  
Author(s):  
Francesco Addeo ◽  
Solange Soulier ◽  
Jean-Pierre Pelissier ◽  
Jean-Marc Chobert ◽  
Jean-Claude Mercier ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Deae Cellulose ◽  
Phosphate Content ◽  
Carbohydrate Composition ◽  
Neuraminic Acids ◽  
Main Fraction ◽  
Carbohydrate Contents

SummaryWhole goat κ-casein was prepared by chromatography of whole casein on hydroxyapatite. Chromatography of whole κ-casein on DEAE-cellulose separated 5 fractions. All of them were sensitive to chymosin. Their amino acid and carbohydrate composition, phosphate content and molecular weight were determined. Galactose, N-acetylgalactosamine, N-acetyl and N-glycolyl neuraminic acids were identified in whole κ-casein. It appears that goat κ-casein, like cow, buffalo and ewe κ-caseins, is composed of several fractions having identical peptide chains and differing in their carbohydrate contents. The main fraction, devoid of carbohydrate, was treated with chymosin. The para-κ-casein and caseinomacropeptide were isolated. Their amino acid composition and phosphate content were determined.

scholarly journals Effect of cooking, pH and polyphenol level on carbohydrate composition and nutritional quality of a sorghum (Sorghum bicolor (L.) Moench) food, ugali

1988 ◽  
Vol 59 (1) ◽  
pp. 31-47 ◽  
Author(s):  
K. E. Bach Knudsen ◽  
L. Munck ◽  
B. O. Eggum
Keyword(s):  
Amino Acid ◽  
Sorghum Bicolor ◽  
Nutritional Quality ◽  
Amino Acid Content ◽  
Carbohydrate Composition ◽  
Dietary Polyphenols ◽  
Endosperm Protein

1. The present work was undertaken to study the effects of cooking, pH and polyphenol level on carbohydrate composition and nutritional quality of sorghum (Sorghum bicolor (L.) Moench). Three different sorghum varieties; Dabar, Feterita and Argentine containing zero, intermediate to low and high levels of polyphenols respectively were used in the study. From these varieties uncooked, uncooked acidified, cooked, and cooked acidified diets were prepared. Diets were characterized with regard to resistant starch (RS), dietary fibre (DF), acid-detergent fibre (ADF) and amino acid content. Raw materials were further analysed for content and composition of non-starch polysaccharides and Klason lignin. The nutritional properties were studied in balance trials with rats. True protein digestibility (TD), biological value (BV), net protein utilization, digestible amino acids, digestible energy (DE) and digestible DF were used as criteria in the nutritional study.2. Cooking at neutral and acid pH resulted in significantly higher assayed values for DF. Increase in DF could be accounted for by formation of RS. Approximately 50% of RS was recovered in the faeces.3. In vitro values for protein associated with ADF and in vivo balance values using rats suggest that an endosperm protein fraction, kafirins, was made unavailable during cooking. This resulted in reduced TD and increased BV. It is assumed that unavailable kafirins serve as a nitrogen source for microflora in the hind-gut.4. Dietary polyphenols changed the excretory route for N from urine to faeces. This resulted in lower TD and higher BV in Argentine (high in polyphenols) than in Dabar and Feterita (low in polyphenols), although dietary lysine (first limiting amino acid) was the same in the three varieties.5. Variation in DE of the diets was attributed to DF, RS and the amount of faecal protein, which in turn were influenced by undigested kafirins and polyphenols.

Carbohydrate Composition And Catabolism Of Five Abnormal Fibrinogens

1981 ◽  
Author(s):  
D A Lane ◽  
A K Allen ◽  
J Markwick ◽  
I Mackie ◽  
E Thompson ◽  
...  
Keyword(s):  
New Zealand ◽  
Sialic Acid ◽  
Amino Acid ◽  
Amino Acid Analysis ◽  
Amino Sugars ◽  
Carbohydrate Composition ◽  
Analysis Techniques ◽  
New Zealand White Rabbits ◽  
Neutral Sugars ◽  
The Mean

An investigation has been made of the carbohydrate composition and catabolism of five abnormal fibrinogens. These were fibrinogens, London, Manchester, Oslo II, a fetal fibrinogen isolated from pooled cord blood and a newly discovered case of hypodysfibrinogenemia which has been tentatively designated fibrinogen London II. The carbohydrate composition of fibrinogen (mol sugar/mol of fibrinogen) was studied by amino acid analysis techniques for amino sugars and methanolysis followed by GLC for neutral sugars and sialic acid. The adult variants did not differ significantly from the normal adult fibrinogen which typically contained 22 mannose, 18 galactose, 20 N-acetylglucosamine, 4 N-acetyl- galactosamine and 12 sialic acid residues. However, fetal fibrinogen was markedly different, containing 15 mannose, 21 galactose, 14 N-acetylglucosamine, 20 N-acetylgalactosamine and 20 sialic acid residues. The catabolism of the I125- labelled fibrinogens was studied in New Zealand White rabbits. Normal fibrinogen was eliminated with a mean t1/2 of 50.2 h (n = 5, range 42-60). The mean t1/2 of fetal fibrinogen was similar 47.7 h (n = 5, range 41-70) and fibrinogens London, London II, Manchester and Oslo II had t1/2’s of 39, 42, 38 and 44 h respectively. It is concluded that (a) the increased sialic acid on fetal fibrinogen is probably due to there being more O-glycosylated serine or threonine residues and this does not alter catabolism, (b) the reduced plasma fbgen of London II is caused by impaired synthesis rather than hypercatabolism, and (c) the catabolism of fibrinogen is only minimally dependent upon the full integrity of the regions of the molecules involved in polymerisation and fibrinopeptide releasing functions.

Effects of mermithid parasitism on the haemolymph composition of the larval blackflies Prosimulium mixtum/fuscum and Simulium venustum

Parasitology ◽  
1978 ◽  
Vol 77 (3) ◽  
pp. 367-374 ◽  
Author(s):  
R. Gordon ◽  
W. J. Condon ◽  
W. J. Edgar ◽  
Sally J. Babie
Keyword(s):  
Amino Acid ◽  
Host Species ◽  
Protein Fractions ◽  
Nutritional Requirements ◽  
Carbohydrate Composition ◽  
Protein Amino Acid ◽  
Glucose Levels ◽  
Amino Compounds ◽  
Mermithid Nematode

SummaryHaemolymph of larval blackflies Prosimulium mixtum/fuscum and Simulium venustum parasitized by the mermithid nematode Neomesomermis flumenalis was compared with that of non-parasitized hosts with respect to protein, amino acid and carbohydrate composition. The mermithid depleted most protein fractions in a non-selective manner in both host species. In P. mixtum/fuscum, the levels of most amino compounds were reduced by mermithid parasitism, but these metabolites were approximately evenly divided into three categories (decreased, increased, unaffected by parasitism) in S. venustum. The mermithid caused a significant decrease of haemolymph glucose levels in both host species but did not affect blood trehalose concentrations. These effects of parasitism are discussed in relation to the nematode's nutritional requirements.

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