Clearing factor and lipase

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Clearing Factor, a Heparin-activated Lipoprotein Lipase

In the first paper of this series (l), evidence was presented which demonstrates that the clearing factor which appears in postheparin plasma is present in the hearts of normal, non-heparinized rats. This strongly supports the view that the enzyme functions in normal fat metabolism. In this paper, the substrate specificity of lipoprotein lipase is defined, the conversion of coconut oil into an ...

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Absence of lipemia clearing factor lipase in human adipose tissue.

Lipoprotein lipase, or lipemia clearing factor lipase (which is more accurate terminology [l]) , is a heparin-activated enzyme which has been found in rat, beef, and pig heart (2). The adipose tissues of rats, rabbits, and especially chickens contain greater quantities of the enzyme (3). This latter observation led to the suggestion that the major site of lipoprotein lipase activity was in the ...

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The lipoprotein lipase (clearing-factor lipase) activity of bovine subcutaneous adipose tissue and isolated adipocytes [proceedings].

Kane, J. P., Sata, T., Hamilton, R. L. & Havel, R. J . (1975) J. Clin. I n i ~ s t . 56, 1622-1634 Langer, T., Strober, W. &Levy, R. 1. (1972)J. Clin. Invest. 51, 1528-1536 Lowry, 0 . H., Rosebrough, N. J., Farr, A. L. & Randall, R . J. ( I 95 I ) J . Bid. Cham. 193,265-275 Matthews, C. M. E. (1957) Phys. Med. B i d . 2, 36-53 Miller, G. J. & Miller, N. E. (1975) Lancer i , 16-19 Packard, C. J....

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The inhibition in vivo of lipoprotein lipase (clearing-factor lipase) activity by triton WR-1339.

1. Lipoprotein lipase activity was measured in heart homogenates and in heparin-releasable and non-releasable fractions of isolated perfused rat hearts, after the intravenous injection of Triton WR-1339. 2. In homogenates of hearts from starved, rats, lipoprotein lipase activity was significantly inhibited (P less than 0.001) 2h after the injection of Triton. This inhibition was restricted excl...

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Stability of lipoprotein lipase (clearing-factor lipase) in rat cardiac muscle [proceedings].

reticulum might suggest that addition of N-acetylglucosamine to the asparagine residue occurs while the nascent protein is associated with polyribosomes. But final conclusions must await information concerning the substrate specificity of UDP-N-acetylglucosamine-asparagine sequon N-acetyl-B-D-glucosaminyltransferase and its mechanism of action. The enzyme in the rough endoplasmic reticulum, bei...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1955

ISSN: 0306-3283

DOI: 10.1042/bj0600665