Introduction of a chiral centre on C-6 of a carbohydrate unit: Application to the synthesis of the C-2 to C-15 fragment of lonomycin

Tetrahedron ◽  
1991 ◽  
Vol 47 (16-17) ◽  
pp. 2733-2750 ◽  
Author(s):  
Deborah Anne Nicoll-Griffith ◽  
Larry Weiler
Keyword(s):  
Carbohydrate Unit

scholarly journals Characterization of a novel pyruvylated carbohydrate unit implicated in the cell aggregation of the marine sponge Microciona prolifera

1993 ◽  
Vol 268 (18) ◽  
pp. 13378-13387
Author(s):  
D. Spillmann ◽  
K. Hård ◽  
J. Thomas-Oates ◽  
J.F. Vliegenthart ◽  
G. Misevic ◽  
...  
Keyword(s):  
Marine Sponge ◽  
Cell Aggregation ◽  
Carbohydrate Unit

Additional Insulin for Coping with Fat- and Protein-Rich Meals in Adolescents with Type 1 Diabetes: The Protein Unit

2020 ◽  
Author(s):  
Roland Schweizer ◽  
Susann Herrlich ◽  
Martina Lösch-Binder ◽  
Michaela Glökler ◽  
Magdalena Heimgärtner ◽  
...  
Keyword(s):  
Type 1 Diabetes ◽  
G Protein ◽  
Insulin Dose ◽  
Dietary Fats ◽  
Target Range ◽  
Pump Therapy ◽  
Glucose Levels ◽  
Protein Rich ◽  
Carbohydrate Unit

Abstract Objective Dietary proteins raise blood glucose levels; dietary fats delay this rise. We sought to assess the insulin amount required to normalize glucose levels after a fat- and protein-rich meal (FPRM). Methods Sixteen adolescents (5 female) with type 1 diabetes (median age: 18.2 years; range: 15.2–24.0; duration: 7.1 years; 2.3–14.3; HbA1c: 7.2%; 6.2–8.3%) were included. FPRM (carbohydrates 57 g; protein 92 g; fat 39 g; fibers 7 g; calories 975 Kcal) was served in the evening, with 20 or 40% extra insulin compared to a standard meal (SM) (carbohydrates 70 g; protein 28 g; fat 19 g; fibers 10 g; calories 579 Kcal) or carbohydrates only. Insulin was administered for patients on intensified insulin therapy or as a 4-hour-delayed bolus for those on pump therapy. The 12-hour post-meal glucose levels were compared between FPRM and SM, with the extra insulin amount calculated based on 100 g proteins as a multiple of the carbohydrate unit. Results Glucose levels (median, mg/dL) 12-hour post-meal with 20% extra insulin vs. 40% vs. insulin dose for SM were 116 vs. 113 vs. 91. Glucose-AUC over 12-hour post-meal with 20% extra insulin vs. 40% vs. insulin dose for SM was 1603 mg/dL/12 h vs. 1527 vs. 1400 (no significance). Glucose levels in the target range with 20% extra insulin vs. 40% were 60% vs. 69% (p=0.1). Glucose levels <60 mg/dL did not increase with 40% extra insulin. This corresponds to the 2.15-fold carbohydrate unit for 100 g protein. Conclusions We recommend administering the same insulin dose given for 1 carbohydrate unit (10 g carbs) to cover 50 g protein.

scholarly journals Characterization of a Novel Sulfated Carbohydrate Unit Implicated in the Carbohydrate-Carbohydrate-mediated Cell Aggregation of the Marine SpongeMicrociona prolifera

1995 ◽  
Vol 270 (10) ◽  
pp. 5089-5097 ◽  
Author(s):  
Dorothe Spillmann ◽  
Jane E. Thomas-Oates ◽  
J. Albert van Kuik ◽  
Johannes F. G. Vliegenthart ◽  
Gradimir Misevic ◽  
...  
Keyword(s):  
Cell Aggregation ◽  
Sulfated Carbohydrate ◽  
Carbohydrate Unit

Glycosylation of chicken haptoglobin: Isolation and characterization of three molecular variants and studies of their distribution in hen plasma before and after turpentine-induced inflammation

1988 ◽  
Vol 66 (3) ◽  
pp. 208-217 ◽  
Author(s):  
Francisco Delers ◽  
Gérard Strecker ◽  
Robert Engler
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Isolation And Characterization ◽  
Molecular Variants ◽  
Hemoglobin Binding ◽  
Significant Difference ◽  
Before And After ◽  
Carbohydrate Unit

Chicken haptoglobin (Hp), a hemoglobin-binding protein isolated from chicken plasma, is composed of three molecular variants that react differently with concanavalin A (ConA). These glycosylation variants of chicken Hp have been isolated by affinity chromatography using Sepharose-bound ConA. They differ in their molecular weight, as determined by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. Analysis of the glycopeptides obtained after pronase digestion of these variants yielded two types of structures: one, reactive with ConA, corresponded to a biantennary N-linked carbohydrate unit and one, unreactive with ConA, corresponded to a triantennary unit. The strongly ConA-reactive Hp variant bears only two biantennary units and the nonreactive Hp variant bears only two triantennary units; the weakly reactive Hp variant bears equal amounts of both units. The distribution of Hp glycosylation variant does not show any significant difference when obtained from the plasma of laying hens before and after turpentine-induced inflammation.

scholarly journals The structure of carbohydrate unit B of porcine thyroglobulin

1981 ◽  
Vol 195 (3) ◽  
pp. 701-713 ◽  
Author(s):  
K Yamamoto ◽  
T Tsuji ◽  
T Irimura ◽  
T Osawa
Keyword(s):  
Sialic Acid ◽  
Concanavalin A ◽  
Deae Cellulose ◽  
Structural Features ◽  
The Other ◽  
Methylation Analysis ◽  
Complex Type ◽  
Mannose Residue ◽  
Sugar Chains ◽  
Carbohydrate Unit

The oligosaccharide fraction was obtained from porcine thyroglobulin by hydrazinolysis. Four fractions of unit B-type oligosaccharides were purified by successive chromatographies on columns of DEAE-cellulose and concanavalin A-Sepharose, and their structures were investigated by the combination of endo- and exo-glycosidase digestions, methylation analysis and Smith degradation. From the results of these studies, the structures of the unit B oligosaccharides were proposed to be as follows: see formula in text. Thus the glycoprotein was found to have triantennary and biantennary complex-type oligosaccharides as acidic sugar chains. Concerning the triantennary oligosaccharides, the following structural features were shown: (1) the sialic acid residues were not localized on certain specific branches but distributed on all three branches; (2) however, alpha (2 leads to 3)-linked sialic acid residues were exclusively located on the terminal of the branch arising from C-4 of the branching alpha-mannose residue, whereas alpha (2 leads to 6)-linked sialic acid residues occupied terminals of the other branches; (3) the outer branching alpha-mannose residue was attached to C-3 or C-6 of an inner branching beta-linked mannose residue, and both types were observed to exist.

scholarly journals Types of oligosaccharide sulphation, depending on mucus glycoprotein source, corpus or antral, in rat stomach

1989 ◽  
Vol 264 (3) ◽  
pp. 805-812 ◽  
Author(s):  
Y Goso ◽  
K Hotta
Keyword(s):  
Chain Length ◽  
Culture Medium ◽  
Gel Filtration ◽  
Rat Stomach ◽  
Mucus Glycoprotein ◽  
Carbohydrate Unit

Radiolabelled mucus glycoprotein was obtained from tissue and a culture medium each of the corpus and antrum of rat stomach incubated with [35S]sulphate in vitro. Gel-filtration analysis of oligosaccharides liberated by alkaline-borohydride treatment from glycoproteins indicated that 35S-labelled oligosaccharides from the corpus vary considerably with respect to chain length whereas those from antral mucus glycoprotein are composed of small oligosaccharides. Examination of the reduced radiolabelled products obtained by HNO2 cleavage of the hydrazine-treated oligosaccharides indicated sulphate esters of N-acetylglucosamine to be present at three locations on a carbohydrate unit: [35S]sulphated monosaccharide (2,5-anhydromannitol 6-sulphate), [35S]sulphated disaccharide [galactosyl(beta 1-4)-2,5-anhydromannitol 6-sulphate] and [35S]sulphated trisaccharide [fucosyl(alpha 1-2)-galactosyl(beta 1-4)-2,5-anhydromannitol 6-sulphate]. Sulphated disaccharide and trisaccharide, possibly originating from the N-acetyl-lactosamine and fucosyl-N-acetyl-lactosamine sequences respectively, were detected in the corpus, especially as large oligosaccharides, but were present in the antrum in only very small amounts. The sulphated monosaccharide, however, most probably originating from 6-sulphated N-acetylglucosamine residues at non-reducing termini, was present in all oligosaccharide fractions in both the corpus and antrum.

scholarly journals The structure of the asparagine-linked carbohydrate unit of rat alpha-lactalbumin.

1980 ◽  
Vol 255 (4) ◽  
pp. 1248-1251
Author(s):  
R. Prasad ◽  
B.G. Hudson ◽  
D.K. Strickland ◽  
K.E. Ebner
Keyword(s):  
Carbohydrate Unit ◽  
Alpha Lactalbumin
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