Purification and characterization of sialic acid containing materials accumulated in cultured skin fibroblasts from a patient with type II sialidosis

1987 ◽  
Vol 10 (1) ◽  
pp. 33-47
Author(s):  
J. R. Scocca ◽  
G. H. Thomas ◽  
C. Miller ◽  
L. Reynolds
Keyword(s):  
Sialic Acid ◽  
Skin Fibroblasts ◽  
Type Ii ◽  
Purification And Characterization ◽  
Cultured Skin

Vitamin D-dependent rickets type II: Studies of the molecular basis of the disease using cultured skin fibroblasts

Bone ◽  
1985 ◽  
Vol 6 (1) ◽  
pp. 55-56
Author(s):  
L.J. Fraher ◽  
G.N. Hendy ◽  
H. Jani ◽  
L. Nicholson ◽  
F.R.J. Hinde ◽  
...  
Keyword(s):  
Vitamin D ◽  
Molecular Basis ◽  
Skin Fibroblasts ◽  
Type Ii ◽  
Cultured Skin

Purification and characterization of cystathionine gamma-synthase type II from Bacillus sphaericus

1987 ◽  
Vol 163 (1) ◽  
pp. 105-112 ◽  
Author(s):  
Hiroshi KANZAKI ◽  
Michihiko KOBAYASHI ◽  
Toru NAGASAWA ◽  
Hideaki YAMADA
Keyword(s):  
Bacillus Sphaericus ◽  
Type Ii ◽  
Purification And Characterization

scholarly journals Purification and characterization of a differentiation-specific sialoglycoprotein of lactating-guinea-pig mammary tissue

1988 ◽  
Vol 251 (2) ◽  
pp. 507-514 ◽  
Author(s):  
V G Johnson ◽  
D E Greenwalt ◽  
P J Madara ◽  
I H Mather
Keyword(s):  
Sialic Acid ◽  
Guinea Pig ◽  
T Antigen ◽  
Mammary Tissue ◽  
Secretory Cells ◽  
Apical Surface ◽  
Mammary Cells ◽  
Purification And Characterization ◽  
Fat Globule

A large acidic glycoprotein, PAS-I, was purified from the fat-globule membrane of guinea-pig milk. Threonine and serine accounted for over 30 mol% of the amino acids, and galactose, N-acetylgalactosamine, N-acetylglucosamine, mannose and sialic acid were the principal sugars detected. On a molar basis, sialic acid accounted for over 60% of the total sugar. Removal of sialic acid by treatment with neuraminidase revealed the presence of binding sites for peanut (Arachis hypogaea) agglutinin, a lectin specific for the sugar sequence beta-D-Gal-(beta 1→3)-D-GalNac (the T antigen). The distribution of PAS-I-related epitopes, defined by five monoclonal antibodies, was determined in the mammary gland and in other guinea-pig tissues. PAS-I was maximally expressed on the apical surfaces of secretory cells in lactating mammary tissue and was either absent, or present in much lower amounts, in the glands of virgin or pregnant animals. PAS-I epitopes were not detected in liver, heart, spleen, pancreas, ovary, uterus, lung or intestine, either by immunofluorescence microscopy or by immunoblotting techniques. Several of the PAS-I-specific antibodies bound to mucins of high Mr in human fat-globule membrane, and similarities and differences between PAS-I and the human mucins are discussed. PAS-I and epitopes of this glycoprotein will be useful as indicators of differentiation in mammary cells and of markers of the apical surface of these cells during lactation.

Expression, Purification, and Characterization of Human Type II Arginase

2001 ◽  
Vol 389 (1) ◽  
pp. 135-143 ◽  
Author(s):  
Diana M. Colleluori ◽  
Sidney M. Morris ◽  
David E. Ash
Keyword(s):  
Type Ii ◽  
Purification And Characterization ◽  
Human Type

scholarly journals Characterization of lysosomes and lysosomal enzymes from Chediak-Higashi-syndrome cultured fibroblasts

1986 ◽  
Vol 238 (2) ◽  
pp. 589-595 ◽  
Author(s):  
A L Miller ◽  
R Stein ◽  
M Sundsmo ◽  
R Y Yeh
Keyword(s):  
Lysosomal Enzymes ◽  
Specific Activity ◽  
Skin Fibroblasts ◽  
Cultured Fibroblasts ◽  
Cultured Skin ◽  
Lysosomal Dysfunction ◽  
Chediak Higashi Syndrome ◽  
Normal Controls

Chediak-Higashi-syndrome cultured skin fibroblasts were used to study the possible involvement of lysosomal enzymes and lysosomal dysfunction in this disorder. Our evidence indicated that Chediak-Higashi fibroblasts displayed a significant decrease in the specific activity of the acidic alpha-D-mannosidase (pH 4.2) compared with normal controls. Additional studies revealed a small, but significant, decrease in the rate of degradation of 125I-labelled beta-D-glucosidase that had been endocytosed into Chediak-Higashi cells.

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