Stability of Complex Carbohydrate Structures

2012 ◽  
Keyword(s):  
Complex Carbohydrate

Effects on Serum Lipids of Different Dietary Fats Associated with a High Sucrose Diet

1973 ◽  
Vol 44 (6) ◽  
pp. 601-604 ◽  
Author(s):  
J. I. Mann ◽  
G. S. Watermeyer ◽  
E. B. Manning ◽  
J. Randles ◽  
A. S. Truswell
Keyword(s):  
Serum Lipids ◽  
Saturated Fat ◽  
Dietary Fats ◽  
Complex Carbohydrate ◽  
The Third ◽  
Sucrose Diet ◽  
Daily Energy ◽  
Dietary Period ◽  
High Sucrose Diet ◽  
High Sucrose

1. Each of nine volunteers was fed three different diets. The percentage of total daily energy provided by fat, carbohydrate and protein remained constant, but the nature of the fat and carbohydrate was altered. The first diet contained ordinary amounts of sucrose and predominantly saturated fat. During the second dietary period, fat remained saturated, but the quantity of sucrose was increased at the expense of complex carbohydrate. In the third dietary period, the sucrose intake remained high, but fat was supplied chiefly in the polyunsaturated form. 2. A small but statistically significant increase of serum fasting cholesterol and triglyceride was observed during the second dietary period, but on the third diet levels of both lipids fell to concentrations not significantly different from those seen on the first diet.

Complex Carbohydrate Composition of Large Dense-Cored Vesicles from Sympathetic Nerve

1987 ◽  
Vol 49 (6) ◽  
pp. 1839-1844 ◽  
Author(s):  
R. U. Margolis ◽  
R. W. Ledeen ◽  
M. Sbaschnig-Agler ◽  
M. C. Byrne ◽  
R. L. Klein ◽  
...  
Keyword(s):  
Sympathetic Nerve ◽  
Carbohydrate Composition ◽  
Complex Carbohydrate

Identification of canine pulmonary surfactant-associated glycoprotein A precursors

1985 ◽  
Vol 58 (6) ◽  
pp. 2091-2095 ◽  
Author(s):  
T. E. Weaver ◽  
J. A. Whitsett ◽  
W. M. Hull ◽  
G. Ross
Keyword(s):  
Gel Electrophoresis ◽  
Pulmonary Surfactant ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Surfactant Protein ◽  
Lung Lavage ◽  
Complex Carbohydrate ◽  
Monospecific Antiserum ◽  
Microsomal Membranes

Surfactant-associated glycoproteins A were identified by two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis of crude surfactant from canine alveolar lavage: an unglycosylated form (protein A1), 27,000–28,000 daltons; glycoprotein A2, 32,000–34,000 daltons; and glycoprotein A3, 37,000–38,000 daltons; pH at isoelectric point (pI) 4.5–5.0. Glycoproteins A2 and A3 were electroeluted and used to prepare a monospecific antiserum that identified proteins A1, A2, and A3 in immunoblots of crude surfactant obtained from dog lung lavage. This antiserum precipitated several proteins from in vitro translated canine lung poly(A)+ mRNA; proteins of 27,000 daltons, pI 5.0, and 28,000 daltons, pI 4.8–5.0, which precisely comigrated with proteins A1 from canine surfactant. Cotranslational processing of the primary translation products by canine pancreatic microsomal membranes resulted in larger proteins of 31,000–34,000 daltons, pI 4.8–5.0. Treatment of these processed forms of glycoprotein A with endoglycosidase F, to remove N-linked carbohydrate, resulted in proteins of 27,000–28,000 daltons which precisely comigrated with surfactant protein A1. These observations demonstrate that the polypeptide precursors to the glycoproteins A complex are extensively modified by addition of asparagine N-linked complex carbohydrate and are subsequently secreted as glycoproteins A2 and A3.

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