Explore: Phosphorylase
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Books Results
Source: The Open Library
The Open Library Search Results
Search results from The Open Library
1Storage polyglucosides
By Conference on Storage Polyglucosides New York 1972.
“Storage polyglucosides” Metadata:
- Title: Storage polyglucosides
- Author: ➤ Conference on Storage Polyglucosides New York 1972.
- Language: English
- Number of Pages: Median: 302
- Publisher: New York Academy of Sciences
- Publish Date: 1973
- Publish Location: [New York]
“Storage polyglucosides” Subjects and Themes:
- Subjects: Congresses - Glycogen - Phosphorylase - Starch
Edition Identifiers:
- The Open Library ID: OL5458222M
- Library of Congress Control Number (LCCN): 73160590
Access and General Info:
- First Year Published: 1973
- Is Full Text Available: No
- Is The Book Public: No
- Access Status: No_ebook
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2The kinetic mechanism of polysaccharide phosphorylase from potato
By Guillermo Rafael Sanchez
“The kinetic mechanism of polysaccharide phosphorylase from potato” Metadata:
- Title: ➤ The kinetic mechanism of polysaccharide phosphorylase from potato
- Author: Guillermo Rafael Sanchez
- Language: English
- Number of Pages: Median: 111
- Publish Date: 1970
“The kinetic mechanism of polysaccharide phosphorylase from potato” Subjects and Themes:
- Subjects: Polusaccharide - Phosphorylase - Potatoes
Edition Identifiers:
- The Open Library ID: OL52628805M
- Online Computer Library Center (OCLC) ID: 501390083
Access and General Info:
- First Year Published: 1970
- Is Full Text Available: No
- Is The Book Public: No
- Access Status: No_ebook
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3Changes in the activities of the thymidine phosphorylating enzymes through the cell cycle of tetrahymena pyriformis and the amoeba-flagellate transformation of naegleria gruberi
By Niels Christian Bols
“Changes in the activities of the thymidine phosphorylating enzymes through the cell cycle of tetrahymena pyriformis and the amoeba-flagellate transformation of naegleria gruberi” Metadata:
- Title: ➤ Changes in the activities of the thymidine phosphorylating enzymes through the cell cycle of tetrahymena pyriformis and the amoeba-flagellate transformation of naegleria gruberi
- Author: Niels Christian Bols
- Language: English
- Number of Pages: Median: 197
- Publisher: Sine nomine
- Publish Date: 1975
- Publish Location: [Toronto
“Changes in the activities of the thymidine phosphorylating enzymes through the cell cycle of tetrahymena pyriformis and the amoeba-flagellate transformation of naegleria gruberi” Subjects and Themes:
- Subjects: ➤ Tetrahymena pyriformis - Thymidine - Phosphorylase - Naegleria gruberi - Enzyme synthesis - Metabolism
Edition Identifiers:
- The Open Library ID: OL20715451M
Access and General Info:
- First Year Published: 1975
- Is Full Text Available: No
- Is The Book Public: No
- Access Status: No_ebook
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4Studies on inhibition of GMP synthetase and MTA phosphorylase
By Hesham Rashwan
“Studies on inhibition of GMP synthetase and MTA phosphorylase” Metadata:
- Title: ➤ Studies on inhibition of GMP synthetase and MTA phosphorylase
- Author: Hesham Rashwan
- Language: English
- Number of Pages: Median: 75
- Publish Date: 1986
“Studies on inhibition of GMP synthetase and MTA phosphorylase” Subjects and Themes:
- Subjects: Enzyme inhibitors - Ligases - Phosphorylase
Edition Identifiers:
- The Open Library ID: OL16604173M
Access and General Info:
- First Year Published: 1986
- Is Full Text Available: No
- Is The Book Public: No
- Access Status: No_ebook
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5Phosphorylase activation in different types of rat muscle
By Louis-Jacques Cartier
“Phosphorylase activation in different types of rat muscle” Metadata:
- Title: ➤ Phosphorylase activation in different types of rat muscle
- Author: Louis-Jacques Cartier
- Language: English
- Number of Pages: Median: 61
- Publish Date: 1981
“Phosphorylase activation in different types of rat muscle” Subjects and Themes:
- Subjects: Phosphorylase
Edition Identifiers:
- The Open Library ID: OL16518881M
Access and General Info:
- First Year Published: 1981
- Is Full Text Available: No
- Is The Book Public: No
- Access Status: No_ebook
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6Protection of the active site of purine nucleoside phosphorylase from acid inactivation by hypoxanthine and its analogs
By Chao-tsu Wang
“Protection of the active site of purine nucleoside phosphorylase from acid inactivation by hypoxanthine and its analogs” Metadata:
- Title: ➤ Protection of the active site of purine nucleoside phosphorylase from acid inactivation by hypoxanthine and its analogs
- Author: Chao-tsu Wang
- Language: English
- Number of Pages: Median: 40
- Publisher: Sine nomine
- Publish Date: 1976
- Publish Location: [s.l
“Protection of the active site of purine nucleoside phosphorylase from acid inactivation by hypoxanthine and its analogs” Subjects and Themes:
- Subjects: ➤ Phosphorylase - Nucleosidases - Enzymes - Synthesis - Purines - Purification
Edition Identifiers:
- The Open Library ID: OL22785657M
Access and General Info:
- First Year Published: 1976
- Is Full Text Available: No
- Is The Book Public: No
- Access Status: No_ebook
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7Storage polyglucosides
By Conference on Storage Polyglucosides, New York, 1972
“Storage polyglucosides” Metadata:
- Title: Storage polyglucosides
- Author: ➤ Conference on Storage Polyglucosides, New York, 1972
- Language: English
- Number of Pages: Median: 302
- Publisher: Academy of Sciences
- Publish Date: 1973
- Publish Location: [New York] New York
“Storage polyglucosides” Subjects and Themes:
- Subjects: Congresses - Glycogen - Phosphorylase - Starch
Edition Identifiers:
- The Open Library ID: OL19158980M
Access and General Info:
- First Year Published: 1973
- Is Full Text Available: No
- Is The Book Public: No
- Access Status: No_ebook
Online Marketplaces
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- Amazon: Audiable, Kindle and printed editions.
- Ebay: New & used books.
Wiki
Source: Wikipedia
Wikipedia Results
Search Results from Wikipedia
Glycogen phosphorylase
Glycogen phosphorylase is one of the phosphorylase enzymes (EC 2.4.1.1). Glycogen phosphorylase catalyzes the rate-limiting step in glycogenolysis in animals
Phosphorylase
In biochemistry, phosphorylases are enzymes that catalyze the addition of a phosphate group from an inorganic phosphate (phosphate+hydrogen) to an acceptor
Earl Wilbur Sutherland Jr.
or Medicine. Sutherland helped to identify the importance of liver phosphorylase (LP) in the process of glycogenolysis. Of the three basic enzymes involved
Purine nucleoside phosphorylase
Purine nucleoside phosphorylase, PNP, PNPase or inosine phosphorylase (EC 2.4.2.1) is an enzyme that in humans is encoded by the NP gene. It catalyzes
Phosphorylase kinase
Phosphorylase kinase (PhK) is a serine/threonine-specific protein kinase which activates glycogen phosphorylase to release glucose-1-phosphate from glycogen
Thymidine phosphorylase
Thymidine phosphorylase (EC 2.4.2.4) is an enzyme that is encoded by the TYMP gene and catalyzes the reaction: thymidine + phosphate ⇌ {\displaystyle
Glycogenolysis
phosphorolysis, by the enzyme glycogen phosphorylase. In the muscles, glycogenolysis begins due to the binding of cAMP to phosphorylase kinase, converting the latter
1,3-beta-oligoglucan phosphorylase
In enzymology, a 1,3-beta-oligoglucan phosphorylase (EC 2.4.1.30) is an enzyme that catalyzes the chemical reaction (1,3-beta-D-glucosyl)n + phosphate
Sucrose phosphorylase
phosphorylase (EC 2.4.1.7) is an important enzyme in the metabolism of sucrose and regulation of other metabolic intermediates. Sucrose phosphorylase
Starch phosphorylase
Starch phosphorylase is a form of phosphorylase similar to glycogen phosphorylase, except that it acts upon starch instead of glycogen. The plant alpha-glucan