Multiple molecular forms of rat brain enkephalinase.

Area of Science:

• Biochemistry
• Neuroscience
• Enzyme Purification

Background:

• Enkephalinase plays a crucial role in neuropeptide metabolism.
• Understanding the molecular forms of enkephalinase is key to elucidating its function.

Purpose of the Study:

• To partially purify rat brain enkephalinase.
• To characterize the different molecular forms of the enzyme.

Main Methods:

• Ion exchange chromatography
• Chromatofocusing
• Affinity chromatography using immobilized lectins (lentil and wheat germ)

Main Results:

• Two principle forms of enkephalinase (A1 and A2) were resolved by ion exchange chromatography.
• Both A1 and A2 bound to immobilized lentil lectin.
• Immobilized wheat germ lectin chromatography resolved A1 and A2 into two subforms each, resulting in four distinct forms: A1,1, A1,2, A2,1, and A2,2.
• All four identified enkephalinase forms exhibited similar kinetic properties.

Conclusions:

• Rat brain enkephalinase exists in multiple molecular forms.
• These forms share similar kinetic properties, suggesting potential post-translational modifications or differential expression.
• The existence of multiple enkephalinase forms may have implications for the regulation of enkephalinergic neurotransmission.