(1985). Molybdenum Hydroxylases as Drug-Metabolizing Enzymes. Drug Metabolism Reviews: Vol. 16, No. 1-2, pp. 119-156.

Molybdenum Hydroxylases as Drug-Metabolizing Enzymes

Conformationally restricted cyclic analogues of substance P: Insight into the receptor binding process

An approach to the self regulatory mechanism of substance P actions: II. Biological activity of new synthetic peptide analogs related both to enkephalin and substance P.

Increasingly, pain is being recognized as a major medical problem. Pain is defined by the International Association for the Study of Pain (IASP) as “an unpleasant sensory and emotional experience associated with actual or potential tissue damage, or described in terms of such damage”1. Pain is always subjective. Each individual learns the application of the word through experiences related to injury in early life1. Pain is widely underestimated and undertreated. In Western countries, 10% of population have acute or chronic pain, and up to 30% of those with disabilities suffer from chronic pain2. The most common types of chronic noncancer pain are arthritis, low back pain, other musculoskeletal pain or stiffness, and fibromyalgia. Chronic pain, defined by the IASP as “pain that persists beyond the normal time of healing... ”3, is a significant problem associated with many long-term diseases, including musculoskeletal disorders, various neurological conditions such as diabetic, HIV-related, or postherpetic neuropathies, and cancer. Most patients find oral medications effective. However, some patients with chronic pain have inadequate pain relief, intolerable side effects, progressive lack of efficacy (tolerance) or allergy associated with oral medications4.

Advances in analgesic drug design and delivery: a current survey.

The metabolism of carbazeran has been investigated in vitro using liver cytosol from dog, baboon and man. Carbazeran was not metabolized in cytosol prepared from dog liver but was rapidly metabolized to a single product in baboon- and human-liver cytosol. The product was identified as 4-hydroxy carbazeran. The enzyme responsible for the 4-hydroxylation of carbazeran in vitro was shown by the use of inhibitors to be liver aldehyde oxidase. Species differences in the metabolism of carbazeran in vitro correlate well with studies in vivo; these showed that following an oral dose to man and baboon, the compound was almost completely cleared via pre-systemic 4-hydroxylation, whereas in the dog, this metabolic route appeared unimportant.

Oxidative metabolism of carbazeran in vitro by liver cytosol of baboon and man.

F r e s h l y prepared s l i c e s of r a b b i t l i v e r , which i s a p a r t i c u l a r l y r i c h source of aldehyde oxidase, xere incubated with phtha laz ine i n the presence of hydralazine. The oxida t ion of ph tha laz ine was monitore4 b y HgLC over a n i n e t y minute per iod and was found t o b e cons iderably reduced conpared t o c o n t r o l incubat ions cont a i n i n g no drug.

The inhibition of rabbit liver aldehyde oxidase by hydralazine

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The inhibition of rabbit liver aldehyde oxidase by hydralazine