Results 241 to 250 of about 89,565 (294)

Chromatography of lysosomal enzymes

Archives of Biochemistry and Biophysics, 1968
Abstract The soluble fraction of rat liver lysosomes has been chromatographed on DEAE-cellulose, Sephadex G-200, and CM-cellulose. Not all of the lysosomal enzymes measured were separated by chromatography on DEAE-cellulose or Sephadex G-200, although separation into groups of enzymes was possible. CM-cellulose chromatography gave the best resolution.
C, Beck, S, Mahadevan, R, Brightwell, C J, Dillard, A L, Tappel   +4 more
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Lysosomes, Lysosomal Enzymes, and Cancer

1992
Publisher Summary Lysosomes are membrane-enclosed cytoplasmic organelles, which posses an acidic interior that contains many hydrolytic enzymes. Their major function is in the the degradation of macromolecules, which may be cellular or foreign in origin.
M J, Boyer, I F, Tannock
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Lysosomal enzymes in human platelets

Cell Biochemistry and Function, 1985
AbstractIn human freshly prepared platelets the following lysosomal enzymes were studied: α‐mannosidase, α‐fucosidase, β‐galactosidase, β‐glucosidase, β‐glucuronidase, β‐N‐acetylglucosaminidase and acid phosphatase. For each of the examined enzymes the conditions providing maximal activity (pH, buffer), kinetic parameters (saturating substrate ...
G, Leoncini, F, Balestrero, M, Maresca
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Lysosomal enzymes in subretinal fluid

Albrecht von Graefes Archiv f�r Klinische und Experimentelle Ophthalmologie, 1976
Samples of subretinal fluid (SRF) from patients with primary rhegmatogeneous retinal detachment of various duration were studied using standard enzymologic techniques. The protein content in SRF increased with the duration of detachment. The activities of lysosomal enzymes in SRF, which were acid phosphatase, beta-glucuronidase, and cathepsin D, also ...
S, Hayasaka, S, Hara, K, Mizuno
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Lysosomal enzymes in cerebral atrophy

Clinica Chimica Acta, 1976
In seven patients with cerebral atrophy due to pre-senile dementia and/or cerebrovascular disease, the activity of acid phosphatase in lumbar cerebrospinal fluid (CSF) was higher (p less than 0.05) than in six controls. The activity of arylsulphatase and beta-galactosidase in CSF was the same in the two groups.
C M, Yates, A, Urquhart, H, Wilson, D, Davidson, W A, Copland   +4 more
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Lysosomal Enzyme Abnormalities in Keratoconus

Archives of Ophthalmology, 1989
We studied the lysosomal enzyme activities in corneas obtained from 12 patients with keratoconus. Three acid hydrolases--acid phosphatase, acid esterase, and acid lipase--were demonstrated by histochemical staining methods in the epithelium, stroma, and endothelium of corneas with keratoconus and normal human corneas.
S, Sawaguchi, B Y, Yue, J, Sugar, J E, Gilboy   +3 more
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Lysosomal enzyme targeting

Biochemical Society Transactions, 1990
Historical overview I want to express my appreciation to the Biochemical Society for having invited me to deliver the 1989 Jubilee Lecture. It is truly a great honour. The word Jubilee connotes a very special anniversary, and in this spirit I want to impart an historical overview to the Lecture in addition to reviewing my most recent work.
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Antigen catabolism by lysosomal enzymes

Immunochemistry, 1970
Abstract The antigenicity of eight proteins (gelatin, insulin, hemoglobin, egg albumin, human γ-globulin, bovine serum albumin, keyhole limpet hemocyanin (KLH), and tetanus toxin) was compared by quantitative precipitin tests. Degradation of these proteins by lysosomal cathepsins in vitro was measured by estimation of the total amino acids released ...
W L, Ryan, J W, Lee
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Chromatography of lysosomal enzymes on hydroxylapatite

Journal of Chromatography A, 1969
Abstract Soluble proteins were extracted from Triton WR 1339-filled rat liver lysosomes and were chromatographed on hydroxylapatite by stepwise elution with increasing concentrations of phosphate buffer (pH 6.8). The distribution of the activities of the cathepsins A, B, C, and D; β-galactosidase; α-mannosidase; β-glucuronidase; β-N ...
J O, Young, D M, Hanes, A L, Tappel
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Lysosomal sequestration of cytosolic enzymes and lysosomal thiol cathepsins

Advances in Enzyme Regulation, 1985
Cytoplasmic proteins are degraded with different half-lives in vivo. Large parts of proteins are believed to be degraded primarily in autophagic vacuoles-lysosomal system. However, the mechanism by which cell proteins are delivered to lysosomes and whether such a process might be selective for certain cell proteins are still unresolved. We examined the
N, Katunuma, E, Kominami
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